Chlorine in PDB 5g3t: The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Enzymatic activity of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
All present enzymatic activity of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum:
1.4.3.23;
Protein crystallography data
The structure of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum, PDB code: 5g3t
was solved by
J.Krausze,
J.Rabe,
J.Moser,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.99 /
1.80
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
68.090,
89.160,
144.430,
90.00,
92.66,
90.00
|
R / Rfree (%)
|
15.7 /
19.2
|
Other elements in 5g3t:
The structure of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum also contains other interesting chemical elements:
Chlorine Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
11;
Binding sites:
The binding sites of Chlorine atom in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
(pdb code 5g3t). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 11 binding sites of Chlorine where determined in the
The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum, PDB code: 5g3t:
Jump to Chlorine binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Chlorine binding site 1 out
of 11 in 5g3t
Go back to
Chlorine Binding Sites List in 5g3t
Chlorine binding site 1 out
of 11 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl421
b:23.1
occ:1.00
|
H
|
A:HIS361
|
2.3
|
19.6
|
1.0
|
HB3
|
A:TRP359
|
2.9
|
14.0
|
1.0
|
HE3
|
A:TRP359
|
3.0
|
16.4
|
1.0
|
N
|
A:HIS361
|
3.1
|
16.3
|
1.0
|
HB2
|
A:HIS361
|
3.1
|
26.4
|
1.0
|
C
|
A:HIS361
|
3.4
|
13.1
|
1.0
|
HA
|
A:TRP359
|
3.5
|
16.8
|
1.0
|
H
|
A:ALA360
|
3.5
|
14.3
|
1.0
|
HA2
|
A:GLY362
|
3.6
|
13.8
|
1.0
|
N
|
A:ALA360
|
3.6
|
11.9
|
1.0
|
CA
|
A:HIS361
|
3.6
|
16.0
|
1.0
|
O
|
A:HIS361
|
3.6
|
18.8
|
1.0
|
HD3
|
A:ARG46
|
3.7
|
19.8
|
1.0
|
CB
|
A:TRP359
|
3.8
|
11.7
|
1.0
|
C
|
A:TRP359
|
3.8
|
13.2
|
1.0
|
N
|
A:GLY362
|
3.8
|
11.6
|
1.0
|
O
|
A:HOH2051
|
3.8
|
24.8
|
1.0
|
CB
|
A:HIS361
|
3.8
|
22.0
|
1.0
|
CA
|
A:TRP359
|
3.8
|
14.0
|
1.0
|
CE3
|
A:TRP359
|
3.9
|
13.7
|
1.0
|
H
|
A:GLY362
|
4.2
|
13.9
|
1.0
|
O
|
A:HOH2326
|
4.2
|
21.8
|
1.0
|
C
|
A:ALA360
|
4.2
|
15.2
|
1.0
|
CA
|
A:GLY362
|
4.2
|
11.5
|
1.0
|
HB1
|
A:ALA360
|
4.2
|
25.5
|
1.0
|
HD2
|
A:HIS361
|
4.2
|
26.2
|
1.0
|
HB2
|
A:TRP359
|
4.4
|
14.0
|
1.0
|
CA
|
A:ALA360
|
4.4
|
13.8
|
1.0
|
O
|
A:TRP359
|
4.4
|
13.9
|
1.0
|
HG2
|
A:ARG46
|
4.5
|
19.6
|
1.0
|
HB3
|
A:HIS361
|
4.5
|
26.4
|
1.0
|
HA
|
A:HIS361
|
4.6
|
19.2
|
1.0
|
CD2
|
A:TRP359
|
4.6
|
11.8
|
1.0
|
CG
|
A:TRP359
|
4.6
|
9.8
|
1.0
|
CD
|
A:ARG46
|
4.6
|
16.5
|
1.0
|
CG
|
A:HIS361
|
4.7
|
23.7
|
1.0
|
HA3
|
A:GLY362
|
4.8
|
13.8
|
1.0
|
CD2
|
A:HIS361
|
4.8
|
21.9
|
1.0
|
O
|
A:HOH2324
|
4.8
|
33.9
|
1.0
|
CB
|
A:ALA360
|
4.9
|
21.2
|
1.0
|
HG3
|
A:ARG46
|
4.9
|
19.6
|
1.0
|
HZ3
|
A:TRP359
|
4.9
|
17.9
|
1.0
|
CG
|
A:ARG46
|
4.9
|
16.3
|
1.0
|
CZ3
|
A:TRP359
|
4.9
|
14.9
|
1.0
|
O
|
A:HOH2357
|
4.9
|
21.0
|
1.0
|
|
Chlorine binding site 2 out
of 11 in 5g3t
Go back to
Chlorine Binding Sites List in 5g3t
Chlorine binding site 2 out
of 11 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl422
b:28.5
occ:1.00
|
H
|
A:ALA43
|
2.3
|
28.0
|
1.0
|
HE22
|
A:GLN189
|
2.3
|
30.5
|
1.0
|
HZ3
|
A:LYS192
|
2.4
|
34.0
|
1.0
|
O
|
A:HOH2040
|
2.9
|
30.0
|
1.0
|
HA
|
A:GLU42
|
3.0
|
25.8
|
1.0
|
NE2
|
A:GLN189
|
3.1
|
25.4
|
1.0
|
N
|
A:ALA43
|
3.2
|
23.3
|
1.0
|
NZ
|
A:LYS192
|
3.2
|
28.3
|
1.0
|
HB3
|
A:GLU42
|
3.3
|
40.2
|
1.0
|
HZ1
|
A:LYS192
|
3.3
|
34.0
|
1.0
|
HD2
|
A:LYS192
|
3.4
|
28.6
|
1.0
|
HB1
|
A:ALA43
|
3.5
|
20.4
|
1.0
|
HE21
|
A:GLN189
|
3.5
|
30.5
|
1.0
|
CA
|
A:GLU42
|
3.6
|
21.5
|
1.0
|
HD12
|
A:LEU204
|
3.7
|
39.4
|
1.0
|
CB
|
A:GLU42
|
3.8
|
33.5
|
1.0
|
HD11
|
A:LEU204
|
3.8
|
39.4
|
1.0
|
HZ2
|
A:LYS192
|
3.8
|
34.0
|
1.0
|
O
|
A:HOH2225
|
3.9
|
40.8
|
1.0
|
HD3
|
A:LYS192
|
3.9
|
28.6
|
1.0
|
C
|
A:GLU42
|
3.9
|
22.0
|
1.0
|
HB3
|
A:ALA43
|
3.9
|
20.4
|
1.0
|
CD
|
A:LYS192
|
3.9
|
23.8
|
1.0
|
CB
|
A:ALA43
|
4.0
|
17.0
|
1.0
|
CG
|
A:GLU42
|
4.0
|
36.1
|
1.0
|
CE
|
A:LYS192
|
4.0
|
23.4
|
1.0
|
CD
|
A:GLN189
|
4.1
|
40.6
|
1.0
|
CD1
|
A:LEU204
|
4.1
|
32.8
|
1.0
|
CA
|
A:ALA43
|
4.2
|
16.8
|
1.0
|
OE1
|
A:GLN189
|
4.2
|
34.0
|
1.0
|
HE3
|
A:LYS192
|
4.3
|
28.1
|
1.0
|
HD13
|
A:LEU204
|
4.3
|
39.4
|
1.0
|
HB2
|
A:GLU42
|
4.7
|
40.2
|
1.0
|
O
|
A:ALA43
|
4.7
|
18.7
|
1.0
|
O
|
A:GLN41
|
4.8
|
27.9
|
1.0
|
O
|
A:HOH2222
|
4.8
|
44.7
|
1.0
|
HE2
|
A:LYS192
|
4.9
|
28.1
|
1.0
|
C
|
A:ALA43
|
4.9
|
16.7
|
1.0
|
HA
|
A:ALA43
|
4.9
|
20.2
|
1.0
|
HB2
|
A:ALA43
|
4.9
|
20.4
|
1.0
|
N
|
A:GLU42
|
4.9
|
26.3
|
1.0
|
|
Chlorine binding site 3 out
of 11 in 5g3t
Go back to
Chlorine Binding Sites List in 5g3t
Chlorine binding site 3 out
of 11 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl422
b:23.4
occ:1.00
|
H
|
B:HIS97
|
2.4
|
18.9
|
1.0
|
HB3
|
B:HIS97
|
3.1
|
18.6
|
1.0
|
HB2
|
B:SER96
|
3.2
|
24.1
|
1.0
|
N
|
B:HIS97
|
3.2
|
15.7
|
1.0
|
HA
|
B:SER96
|
3.3
|
19.3
|
1.0
|
HB2
|
B:HIS97
|
3.5
|
18.6
|
1.0
|
CB
|
B:HIS97
|
3.7
|
15.5
|
1.0
|
CA
|
B:SER96
|
3.9
|
16.1
|
1.0
|
CB
|
B:SER96
|
3.9
|
20.1
|
1.0
|
C
|
B:SER96
|
4.1
|
16.1
|
1.0
|
CA
|
B:HIS97
|
4.1
|
12.8
|
1.0
|
HB3
|
B:SER96
|
4.3
|
24.1
|
1.0
|
H
|
B:VAL98
|
4.5
|
14.6
|
1.0
|
HA
|
B:HIS97
|
4.7
|
15.3
|
1.0
|
|
Chlorine binding site 4 out
of 11 in 5g3t
Go back to
Chlorine Binding Sites List in 5g3t
Chlorine binding site 4 out
of 11 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 4 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl423
b:25.3
occ:1.00
|
H
|
B:HIS361
|
2.4
|
21.9
|
1.0
|
HB3
|
B:TRP359
|
2.9
|
16.6
|
1.0
|
HE3
|
B:TRP359
|
3.0
|
19.3
|
1.0
|
O
|
A:HOH2108
|
3.1
|
39.0
|
1.0
|
O
|
B:HOH2008
|
3.1
|
37.0
|
1.0
|
N
|
B:HIS361
|
3.2
|
18.3
|
1.0
|
HB2
|
B:HIS361
|
3.3
|
30.8
|
1.0
|
C
|
B:HIS361
|
3.4
|
20.6
|
1.0
|
H
|
B:ALA360
|
3.5
|
17.7
|
1.0
|
HA
|
B:TRP359
|
3.5
|
18.4
|
1.0
|
HA2
|
B:GLY362
|
3.6
|
18.1
|
1.0
|
N
|
B:ALA360
|
3.6
|
14.7
|
1.0
|
CA
|
B:HIS361
|
3.7
|
20.3
|
1.0
|
HD3
|
B:ARG46
|
3.7
|
23.7
|
1.0
|
O
|
B:HIS361
|
3.7
|
20.7
|
1.0
|
CB
|
B:TRP359
|
3.7
|
13.9
|
1.0
|
N
|
B:GLY362
|
3.8
|
14.9
|
1.0
|
C
|
B:TRP359
|
3.8
|
16.9
|
1.0
|
CA
|
B:TRP359
|
3.8
|
15.3
|
1.0
|
CE3
|
B:TRP359
|
3.9
|
16.1
|
1.0
|
CB
|
B:HIS361
|
3.9
|
25.6
|
1.0
|
O
|
B:HOH2043
|
4.0
|
26.0
|
1.0
|
H
|
B:GLY362
|
4.1
|
17.8
|
1.0
|
CA
|
B:GLY362
|
4.2
|
15.1
|
1.0
|
O
|
A:HOH2251
|
4.2
|
24.4
|
1.0
|
C
|
B:ALA360
|
4.2
|
18.3
|
1.0
|
HD2
|
B:HIS361
|
4.3
|
31.1
|
1.0
|
HG2
|
B:ARG46
|
4.3
|
23.7
|
1.0
|
HB1
|
B:ALA360
|
4.3
|
30.2
|
1.0
|
HB2
|
B:TRP359
|
4.4
|
16.6
|
1.0
|
O
|
B:TRP359
|
4.4
|
17.6
|
1.0
|
CA
|
B:ALA360
|
4.4
|
17.3
|
1.0
|
CD
|
B:ARG46
|
4.6
|
19.7
|
1.0
|
CD2
|
B:TRP359
|
4.6
|
14.6
|
1.0
|
CG
|
B:TRP359
|
4.6
|
12.7
|
1.0
|
HA
|
B:HIS361
|
4.6
|
24.4
|
1.0
|
HB3
|
B:HIS361
|
4.6
|
30.8
|
1.0
|
O
|
B:HOH2282
|
4.7
|
42.3
|
1.0
|
CG
|
B:HIS361
|
4.8
|
28.4
|
1.0
|
HA3
|
B:GLY362
|
4.8
|
18.1
|
1.0
|
HG3
|
B:ARG46
|
4.8
|
23.7
|
1.0
|
CG
|
B:ARG46
|
4.8
|
19.8
|
1.0
|
CD2
|
B:HIS361
|
4.8
|
25.9
|
1.0
|
O
|
B:HOH2299
|
4.9
|
25.7
|
1.0
|
HZ3
|
B:TRP359
|
4.9
|
19.3
|
1.0
|
CZ3
|
B:TRP359
|
4.9
|
16.1
|
1.0
|
CB
|
B:ALA360
|
4.9
|
25.2
|
1.0
|
|
Chlorine binding site 5 out
of 11 in 5g3t
Go back to
Chlorine Binding Sites List in 5g3t
Chlorine binding site 5 out
of 11 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 5 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cl420
b:57.1
occ:1.00
|
HH22
|
C:ARG410
|
2.2
|
36.4
|
1.0
|
NH2
|
C:ARG410
|
3.0
|
30.4
|
1.0
|
HH12
|
C:ARG410
|
3.2
|
31.7
|
1.0
|
HH12
|
C:ARG406
|
3.3
|
49.9
|
1.0
|
NH1
|
C:ARG406
|
3.5
|
41.6
|
1.0
|
HH21
|
C:ARG410
|
3.5
|
36.4
|
1.0
|
HH11
|
C:ARG406
|
3.7
|
49.9
|
1.0
|
NH1
|
C:ARG410
|
3.8
|
26.4
|
1.0
|
CZ
|
C:ARG410
|
3.9
|
22.5
|
1.0
|
CZ
|
C:ARG406
|
4.0
|
39.5
|
1.0
|
HH22
|
C:ARG406
|
4.1
|
41.1
|
1.0
|
NH2
|
C:ARG406
|
4.3
|
34.3
|
1.0
|
HD2
|
C:ARG406
|
4.5
|
30.8
|
1.0
|
HH11
|
C:ARG410
|
4.6
|
31.7
|
1.0
|
O
|
C:HOH2347
|
4.7
|
35.9
|
1.0
|
NE
|
C:ARG406
|
4.7
|
33.4
|
1.0
|
HH21
|
C:ARG406
|
4.8
|
41.1
|
1.0
|
O
|
C:HOH2343
|
4.9
|
37.6
|
1.0
|
|
Chlorine binding site 6 out
of 11 in 5g3t
Go back to
Chlorine Binding Sites List in 5g3t
Chlorine binding site 6 out
of 11 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 6 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cl421
b:25.5
occ:1.00
|
H
|
C:HIS97
|
2.3
|
22.9
|
1.0
|
HB3
|
C:HIS97
|
3.2
|
18.3
|
1.0
|
N
|
C:HIS97
|
3.2
|
19.1
|
1.0
|
HB2
|
C:SER96
|
3.2
|
22.0
|
1.0
|
HA
|
C:SER96
|
3.4
|
23.6
|
1.0
|
HB2
|
C:HIS97
|
3.5
|
18.3
|
1.0
|
CB
|
C:HIS97
|
3.7
|
15.3
|
1.0
|
CA
|
C:SER96
|
3.9
|
19.7
|
1.0
|
CB
|
C:SER96
|
4.0
|
18.3
|
1.0
|
C
|
C:SER96
|
4.1
|
21.8
|
1.0
|
CA
|
C:HIS97
|
4.1
|
16.9
|
1.0
|
HB3
|
C:SER96
|
4.4
|
22.0
|
1.0
|
H
|
C:VAL98
|
4.5
|
17.0
|
1.0
|
HA
|
C:HIS97
|
4.7
|
20.3
|
1.0
|
|
Chlorine binding site 7 out
of 11 in 5g3t
Go back to
Chlorine Binding Sites List in 5g3t
Chlorine binding site 7 out
of 11 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 7 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cl422
b:24.2
occ:1.00
|
H
|
C:HIS361
|
2.3
|
18.2
|
1.0
|
O
|
C:HOH2020
|
2.8
|
30.9
|
1.0
|
HE3
|
C:TRP359
|
2.9
|
16.9
|
1.0
|
HB3
|
C:TRP359
|
3.0
|
13.5
|
1.0
|
N
|
C:HIS361
|
3.2
|
15.2
|
1.0
|
HB2
|
C:HIS361
|
3.2
|
24.8
|
1.0
|
H
|
C:ALA360
|
3.4
|
15.4
|
1.0
|
C
|
C:HIS361
|
3.4
|
14.7
|
1.0
|
HA
|
C:TRP359
|
3.5
|
12.9
|
1.0
|
HA2
|
C:GLY362
|
3.6
|
17.8
|
1.0
|
N
|
C:ALA360
|
3.6
|
12.8
|
1.0
|
O
|
C:HIS361
|
3.6
|
18.1
|
1.0
|
HD3
|
C:ARG46
|
3.6
|
20.2
|
1.0
|
CA
|
C:HIS361
|
3.7
|
16.1
|
1.0
|
N
|
C:GLY362
|
3.8
|
13.0
|
1.0
|
C
|
C:TRP359
|
3.8
|
13.7
|
1.0
|
CB
|
C:TRP359
|
3.8
|
11.3
|
1.0
|
CE3
|
C:TRP359
|
3.8
|
14.1
|
1.0
|
CA
|
C:TRP359
|
3.9
|
10.8
|
1.0
|
CB
|
C:HIS361
|
3.9
|
20.7
|
1.0
|
O
|
C:HOH2328
|
4.1
|
20.6
|
1.0
|
H
|
C:GLY362
|
4.2
|
15.7
|
1.0
|
CA
|
C:GLY362
|
4.2
|
14.9
|
1.0
|
C
|
C:ALA360
|
4.2
|
15.7
|
1.0
|
HB1
|
C:ALA360
|
4.3
|
19.8
|
1.0
|
O
|
C:HOH2057
|
4.3
|
25.5
|
1.0
|
HG2
|
C:ARG46
|
4.3
|
16.1
|
1.0
|
HD2
|
C:HIS361
|
4.4
|
28.2
|
1.0
|
CA
|
C:ALA360
|
4.4
|
13.8
|
1.0
|
HB2
|
C:TRP359
|
4.4
|
13.5
|
1.0
|
O
|
C:TRP359
|
4.5
|
13.7
|
1.0
|
CD
|
C:ARG46
|
4.5
|
16.8
|
1.0
|
CD2
|
C:TRP359
|
4.5
|
10.9
|
1.0
|
HA
|
C:HIS361
|
4.6
|
19.4
|
1.0
|
HB3
|
C:HIS361
|
4.6
|
24.8
|
1.0
|
CG
|
C:TRP359
|
4.6
|
10.4
|
1.0
|
O
|
C:HOH2326
|
4.7
|
30.0
|
1.0
|
HG3
|
C:ARG46
|
4.7
|
16.1
|
1.0
|
HZ3
|
C:TRP359
|
4.7
|
16.4
|
1.0
|
CG
|
C:ARG46
|
4.7
|
13.4
|
1.0
|
HA3
|
C:GLY362
|
4.7
|
17.8
|
1.0
|
CZ3
|
C:TRP359
|
4.8
|
13.7
|
1.0
|
CG
|
C:HIS361
|
4.8
|
19.5
|
1.0
|
CB
|
C:ALA360
|
4.9
|
16.5
|
1.0
|
O
|
C:HOH2355
|
4.9
|
22.1
|
1.0
|
CD2
|
C:HIS361
|
4.9
|
23.5
|
1.0
|
|
Chlorine binding site 8 out
of 11 in 5g3t
Go back to
Chlorine Binding Sites List in 5g3t
Chlorine binding site 8 out
of 11 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 8 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cl423
b:26.2
occ:1.00
|
HD21
|
C:ASN293
|
2.5
|
20.6
|
1.0
|
O
|
C:HOH2147
|
2.9
|
33.4
|
1.0
|
HG
|
C:SER339
|
2.9
|
31.5
|
1.0
|
HB3
|
C:ASN293
|
2.9
|
24.5
|
1.0
|
O
|
C:HOH2283
|
3.0
|
16.3
|
1.0
|
HB2
|
C:SER339
|
3.0
|
21.7
|
1.0
|
ND2
|
C:ASN293
|
3.3
|
17.2
|
1.0
|
OG
|
C:SER339
|
3.4
|
26.3
|
1.0
|
HA
|
C:ALA340
|
3.6
|
22.9
|
1.0
|
CB
|
C:SER339
|
3.7
|
18.1
|
1.0
|
O
|
C:SER339
|
3.8
|
21.1
|
1.0
|
C
|
C:SER339
|
3.8
|
23.0
|
1.0
|
CB
|
C:ASN293
|
3.8
|
20.4
|
1.0
|
HD22
|
C:ASN293
|
3.8
|
20.6
|
1.0
|
HB
|
C:VAL291
|
4.0
|
19.6
|
1.0
|
CG
|
C:ASN293
|
4.1
|
17.5
|
1.0
|
N
|
C:ALA340
|
4.1
|
21.1
|
1.0
|
HB2
|
C:ASN293
|
4.1
|
24.5
|
1.0
|
O
|
C:ASP292
|
4.2
|
11.8
|
1.0
|
CA
|
C:ALA340
|
4.3
|
19.1
|
1.0
|
CA
|
C:SER339
|
4.4
|
19.0
|
1.0
|
HB3
|
C:SER339
|
4.5
|
21.7
|
1.0
|
H
|
C:ALA340
|
4.5
|
25.2
|
1.0
|
O
|
C:HOH2282
|
4.5
|
20.9
|
1.0
|
HB3
|
C:ALA340
|
4.6
|
25.5
|
1.0
|
C
|
C:ASP292
|
4.6
|
12.3
|
1.0
|
H
|
C:ASP292
|
4.8
|
15.7
|
1.0
|
HA
|
C:SER339
|
4.8
|
22.8
|
1.0
|
N
|
C:ASN293
|
4.9
|
13.1
|
1.0
|
CA
|
C:ASN293
|
4.9
|
11.8
|
1.0
|
CB
|
C:VAL291
|
5.0
|
16.3
|
1.0
|
|
Chlorine binding site 9 out
of 11 in 5g3t
Go back to
Chlorine Binding Sites List in 5g3t
Chlorine binding site 9 out
of 11 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 9 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cl424
b:25.8
occ:1.00
|
HZ3
|
C:LYS192
|
2.2
|
32.2
|
1.0
|
H
|
C:ALA43
|
2.3
|
21.8
|
1.0
|
HE22
|
C:GLN189
|
2.6
|
27.9
|
1.0
|
HA
|
C:GLU42
|
2.9
|
25.3
|
1.0
|
NZ
|
C:LYS192
|
3.0
|
26.9
|
1.0
|
N
|
C:ALA43
|
3.1
|
18.1
|
1.0
|
HZ1
|
C:LYS192
|
3.2
|
32.2
|
1.0
|
HB3
|
C:GLU42
|
3.4
|
32.4
|
1.0
|
HD2
|
C:LYS192
|
3.4
|
24.4
|
1.0
|
HB1
|
C:ALA43
|
3.4
|
23.2
|
1.0
|
NE2
|
C:GLN189
|
3.4
|
23.2
|
1.0
|
HZ2
|
C:LYS192
|
3.5
|
32.2
|
1.0
|
HD12
|
C:LEU204
|
3.6
|
29.6
|
1.0
|
CA
|
C:GLU42
|
3.6
|
21.1
|
1.0
|
HD11
|
C:LEU204
|
3.7
|
29.6
|
1.0
|
O
|
C:HOH2216
|
3.8
|
36.6
|
1.0
|
HE21
|
C:GLN189
|
3.8
|
27.9
|
1.0
|
HB3
|
C:ALA43
|
3.8
|
23.2
|
1.0
|
CB
|
C:GLU42
|
3.9
|
27.0
|
1.0
|
C
|
C:GLU42
|
3.9
|
21.7
|
1.0
|
CE
|
C:LYS192
|
3.9
|
24.9
|
1.0
|
CD
|
C:LYS192
|
3.9
|
20.4
|
1.0
|
CB
|
C:ALA43
|
3.9
|
19.4
|
1.0
|
HD3
|
C:LYS192
|
4.0
|
24.4
|
1.0
|
CD1
|
C:LEU204
|
4.0
|
24.6
|
1.0
|
CA
|
C:ALA43
|
4.1
|
17.6
|
1.0
|
HE3
|
C:LYS192
|
4.1
|
29.9
|
1.0
|
HD13
|
C:LEU204
|
4.2
|
29.6
|
1.0
|
CG
|
C:GLU42
|
4.2
|
32.4
|
1.0
|
CD
|
C:GLN189
|
4.3
|
39.2
|
1.0
|
OE1
|
C:GLN189
|
4.4
|
27.6
|
1.0
|
O
|
C:ALA43
|
4.7
|
19.7
|
1.0
|
HB2
|
C:GLU42
|
4.8
|
32.4
|
1.0
|
HE2
|
C:LYS192
|
4.8
|
29.9
|
1.0
|
O
|
C:GLN41
|
4.8
|
22.2
|
1.0
|
HA
|
C:ALA43
|
4.8
|
21.1
|
1.0
|
C
|
C:ALA43
|
4.8
|
17.1
|
1.0
|
HB2
|
C:ALA43
|
4.8
|
23.2
|
1.0
|
N
|
C:GLU42
|
4.9
|
19.0
|
1.0
|
|
Chlorine binding site 10 out
of 11 in 5g3t
Go back to
Chlorine Binding Sites List in 5g3t
Chlorine binding site 10 out
of 11 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 10 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cl423
b:27.0
occ:1.00
|
HZ3
|
D:LYS192
|
2.2
|
37.2
|
1.0
|
H
|
D:ALA43
|
2.2
|
20.3
|
1.0
|
HE22
|
D:GLN189
|
2.6
|
30.3
|
1.0
|
HA
|
D:GLU42
|
3.0
|
24.2
|
1.0
|
NZ
|
D:LYS192
|
3.0
|
31.0
|
1.0
|
N
|
D:ALA43
|
3.1
|
16.9
|
1.0
|
HZ1
|
D:LYS192
|
3.2
|
37.2
|
1.0
|
HD2
|
D:LYS192
|
3.2
|
24.5
|
1.0
|
HB1
|
D:ALA43
|
3.2
|
20.9
|
1.0
|
HB3
|
D:GLU42
|
3.4
|
29.6
|
1.0
|
NE2
|
D:GLN189
|
3.4
|
25.2
|
1.0
|
HZ2
|
D:LYS192
|
3.6
|
37.2
|
1.0
|
HD12
|
D:LEU204
|
3.6
|
30.2
|
1.0
|
CA
|
D:GLU42
|
3.7
|
20.2
|
1.0
|
HB3
|
D:ALA43
|
3.7
|
20.9
|
1.0
|
HD11
|
D:LEU204
|
3.7
|
30.2
|
1.0
|
CB
|
D:ALA43
|
3.8
|
17.4
|
1.0
|
HE21
|
D:GLN189
|
3.8
|
30.3
|
1.0
|
CD
|
D:LYS192
|
3.8
|
20.4
|
1.0
|
C
|
D:GLU42
|
3.9
|
17.9
|
1.0
|
CE
|
D:LYS192
|
3.9
|
24.4
|
1.0
|
HD3
|
D:LYS192
|
3.9
|
24.5
|
1.0
|
CB
|
D:GLU42
|
3.9
|
24.7
|
1.0
|
O
|
D:HOH2194
|
3.9
|
37.6
|
1.0
|
CA
|
D:ALA43
|
4.0
|
15.9
|
1.0
|
CD1
|
D:LEU204
|
4.0
|
25.2
|
1.0
|
HE3
|
D:LYS192
|
4.1
|
29.3
|
1.0
|
HD13
|
D:LEU204
|
4.2
|
30.2
|
1.0
|
CD
|
D:GLN189
|
4.4
|
37.6
|
1.0
|
CG
|
D:GLU42
|
4.4
|
33.2
|
1.0
|
OE1
|
D:GLN189
|
4.5
|
32.3
|
1.0
|
O
|
D:HOH2040
|
4.5
|
35.4
|
1.0
|
O
|
D:ALA43
|
4.6
|
18.9
|
1.0
|
HB2
|
D:ALA43
|
4.7
|
20.9
|
1.0
|
HE2
|
D:LYS192
|
4.7
|
29.3
|
1.0
|
HA
|
D:ALA43
|
4.7
|
19.1
|
1.0
|
C
|
D:ALA43
|
4.8
|
16.9
|
1.0
|
HB2
|
D:GLU42
|
4.8
|
29.6
|
1.0
|
O
|
D:GLN41
|
4.8
|
23.7
|
1.0
|
N
|
D:GLU42
|
5.0
|
19.9
|
1.0
|
|
Reference:
J.Fuller,
R.Roepke,
J.Krausze,
K.E.Rennhack,
N.P.Daniel,
W.Blankenfeldt,
S.Schulz,
D.Jahn,
J.Moser.
Biosynthesis of Violacein: Structure and Function of L-Tryptophan Oxidase Vioa Chromobacterium Violaceum J.Biol.Chem. V. 291 20068 2016.
ISSN: ISSN 0021-9258
PubMed: 27466367
DOI: 10.1074/JBC.M116.741561
Page generated: Fri Jul 26 08:20:01 2024
|