Chlorine in PDB 9er5: Hydrogenase-1 Ni-B State Poised at +100MV
Enzymatic activity of Hydrogenase-1 Ni-B State Poised at +100MV
All present enzymatic activity of Hydrogenase-1 Ni-B State Poised at +100MV:
1.12.99.6;
Protein crystallography data
The structure of Hydrogenase-1 Ni-B State Poised at +100MV, PDB code: 9er5
was solved by
S.B.Carr,
W.Li,
K.L.Wong,
P.A.Ash,
K.A.Vincent,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
85.95 /
1.40
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
93.62,
97.36,
182.96,
90,
90,
90
|
R / Rfree (%)
|
15.3 /
17.4
|
Other elements in 9er5:
The structure of Hydrogenase-1 Ni-B State Poised at +100MV also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Hydrogenase-1 Ni-B State Poised at +100MV
(pdb code 9er5). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the
Hydrogenase-1 Ni-B State Poised at +100MV, PDB code: 9er5:
Jump to Chlorine binding site number:
1;
2;
3;
4;
Chlorine binding site 1 out
of 4 in 9er5
Go back to
Chlorine Binding Sites List in 9er5
Chlorine binding site 1 out
of 4 in the Hydrogenase-1 Ni-B State Poised at +100MV
 Mono view
 Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Hydrogenase-1 Ni-B State Poised at +100MV within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Cl404
b:15.8
occ:1.00
|
O
|
S:HOH605
|
3.1
|
21.4
|
1.0
|
N
|
S:CYS120
|
3.1
|
11.6
|
1.0
|
O
|
S:HOH664
|
3.1
|
27.2
|
1.0
|
N
|
S:GLY256
|
3.2
|
13.2
|
1.0
|
CG2
|
S:THR114
|
3.6
|
13.1
|
1.0
|
CA
|
S:CYS120
|
3.7
|
11.2
|
1.0
|
CB
|
S:TRP118
|
3.7
|
14.5
|
1.0
|
CA
|
S:GLY256
|
3.9
|
13.4
|
1.0
|
N
|
S:GLY119
|
4.0
|
12.8
|
1.0
|
C
|
S:GLY119
|
4.1
|
13.2
|
1.0
|
C
|
S:TRP118
|
4.2
|
14.0
|
1.0
|
C
|
S:ASN255
|
4.2
|
11.8
|
1.0
|
OD1
|
S:ASN255
|
4.2
|
15.7
|
1.0
|
CA
|
S:GLY119
|
4.2
|
14.2
|
1.0
|
CA
|
S:ASN255
|
4.2
|
11.9
|
1.0
|
O
|
S:HOH675
|
4.3
|
27.5
|
1.0
|
O
|
S:CYS120
|
4.3
|
11.5
|
1.0
|
O
|
S:GLU254
|
4.4
|
12.0
|
1.0
|
N
|
S:PHE257
|
4.5
|
12.5
|
1.0
|
C
|
S:CYS120
|
4.5
|
11.4
|
1.0
|
O
|
S:TRP118
|
4.5
|
15.0
|
1.0
|
C
|
S:GLY256
|
4.6
|
14.3
|
1.0
|
CA
|
S:TRP118
|
4.6
|
11.9
|
1.0
|
CD1
|
S:TRP258
|
4.6
|
11.3
|
1.0
|
CD1
|
S:PHE257
|
4.7
|
12.6
|
1.0
|
CG
|
S:TRP118
|
4.8
|
15.4
|
1.0
|
CB
|
S:CYS120
|
4.8
|
11.1
|
1.0
|
O
|
S:THR114
|
4.8
|
11.3
|
1.0
|
O
|
S:HOH641
|
4.8
|
27.5
|
1.0
|
|
Chlorine binding site 2 out
of 4 in 9er5
Go back to
Chlorine Binding Sites List in 9er5
Chlorine binding site 2 out
of 4 in the Hydrogenase-1 Ni-B State Poised at +100MV
 Mono view
 Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Hydrogenase-1 Ni-B State Poised at +100MV within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Cl405
b:26.4
occ:1.00
|
O
|
S:HOH633
|
3.0
|
30.8
|
1.0
|
N
|
S:HIS13
|
3.1
|
12.1
|
1.0
|
OD2
|
S:ASP46
|
3.2
|
28.8
|
1.0
|
O
|
S:HOH590
|
3.4
|
26.1
|
1.0
|
CA
|
S:ILE12
|
3.4
|
12.2
|
1.0
|
CB
|
S:ILE12
|
3.4
|
13.0
|
1.0
|
NZ
|
S:LYS98
|
3.5
|
20.8
|
1.0
|
CE
|
S:LYS98
|
3.8
|
20.4
|
1.0
|
C
|
S:ILE12
|
3.8
|
12.7
|
1.0
|
O
|
S:HIS13
|
3.8
|
13.0
|
1.0
|
CG
|
S:ASP46
|
3.8
|
23.7
|
1.0
|
CG2
|
S:ILE12
|
3.8
|
14.0
|
1.0
|
CE1
|
S:TYR44
|
4.0
|
15.8
|
1.0
|
CA
|
S:HIS13
|
4.1
|
12.1
|
1.0
|
OD1
|
S:ASP46
|
4.1
|
23.2
|
1.0
|
CD
|
S:LYS98
|
4.2
|
18.8
|
1.0
|
CB
|
S:HIS13
|
4.2
|
11.9
|
1.0
|
C
|
S:HIS13
|
4.3
|
11.7
|
1.0
|
OH
|
S:TYR44
|
4.4
|
20.4
|
1.0
|
CD2
|
S:HIS13
|
4.5
|
12.4
|
1.0
|
O
|
S:TRP11
|
4.6
|
14.0
|
1.0
|
CZ
|
S:TYR44
|
4.7
|
17.3
|
1.0
|
CE1
|
S:PHE95
|
4.7
|
13.6
|
1.0
|
N
|
S:ILE12
|
4.7
|
12.2
|
1.0
|
CG
|
S:HIS13
|
4.8
|
12.5
|
1.0
|
CG1
|
S:ILE12
|
4.8
|
14.7
|
1.0
|
CB
|
S:ASP46
|
4.8
|
18.1
|
1.0
|
CD1
|
S:TYR44
|
4.9
|
14.3
|
1.0
|
|
Chlorine binding site 3 out
of 4 in 9er5
Go back to
Chlorine Binding Sites List in 9er5
Chlorine binding site 3 out
of 4 in the Hydrogenase-1 Ni-B State Poised at +100MV
 Mono view
 Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of Hydrogenase-1 Ni-B State Poised at +100MV within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
T:Cl404
b:16.1
occ:1.00
|
O
|
T:HOH617
|
3.0
|
18.6
|
1.0
|
O
|
T:HOH662
|
3.1
|
28.0
|
1.0
|
N
|
T:GLY256
|
3.1
|
12.9
|
1.0
|
N
|
T:CYS120
|
3.2
|
12.8
|
1.0
|
CG2
|
T:THR114
|
3.7
|
14.4
|
1.0
|
CA
|
T:CYS120
|
3.7
|
12.9
|
1.0
|
CB
|
T:TRP118
|
3.7
|
16.7
|
1.0
|
CA
|
T:GLY256
|
3.8
|
14.1
|
1.0
|
N
|
T:GLY119
|
4.0
|
12.3
|
1.0
|
C
|
T:ASN255
|
4.1
|
13.8
|
1.0
|
C
|
T:TRP118
|
4.1
|
15.2
|
1.0
|
C
|
T:GLY119
|
4.2
|
12.7
|
1.0
|
CA
|
T:ASN255
|
4.2
|
13.2
|
1.0
|
OD1
|
T:ASN255
|
4.3
|
16.9
|
1.0
|
CA
|
T:GLY119
|
4.3
|
12.4
|
1.0
|
O
|
T:GLU254
|
4.3
|
13.1
|
1.0
|
N
|
T:PHE257
|
4.4
|
12.7
|
1.0
|
O
|
T:CYS120
|
4.4
|
12.4
|
1.0
|
O
|
T:TRP118
|
4.4
|
14.3
|
1.0
|
O
|
T:HOH673
|
4.5
|
26.8
|
1.0
|
C
|
T:CYS120
|
4.5
|
12.8
|
1.0
|
C
|
T:GLY256
|
4.5
|
13.1
|
1.0
|
CA
|
T:TRP118
|
4.6
|
14.2
|
1.0
|
CD1
|
T:TRP258
|
4.6
|
11.8
|
1.0
|
CD1
|
T:PHE257
|
4.6
|
13.0
|
1.0
|
CG
|
T:TRP118
|
4.8
|
17.9
|
1.0
|
CB
|
T:CYS120
|
4.8
|
11.4
|
1.0
|
O
|
T:HOH663
|
4.8
|
28.1
|
1.0
|
O
|
T:THR114
|
4.9
|
12.1
|
1.0
|
|
Chlorine binding site 4 out
of 4 in 9er5
Go back to
Chlorine Binding Sites List in 9er5
Chlorine binding site 4 out
of 4 in the Hydrogenase-1 Ni-B State Poised at +100MV
 Mono view
 Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 4 of Hydrogenase-1 Ni-B State Poised at +100MV within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
T:Cl405
b:29.6
occ:1.00
|
O
|
T:HOH664
|
3.0
|
35.2
|
1.0
|
N
|
T:HIS13
|
3.1
|
12.4
|
1.0
|
OD2
|
T:ASP46
|
3.3
|
29.2
|
1.0
|
O
|
T:HOH580
|
3.3
|
30.6
|
1.0
|
CA
|
T:ILE12
|
3.4
|
13.7
|
1.0
|
CB
|
T:ILE12
|
3.4
|
12.4
|
1.0
|
NZ
|
T:LYS98
|
3.5
|
22.0
|
1.0
|
C
|
T:ILE12
|
3.8
|
13.1
|
1.0
|
CE
|
T:LYS98
|
3.8
|
21.5
|
1.0
|
CG2
|
T:ILE12
|
3.8
|
12.4
|
1.0
|
O
|
T:HIS13
|
3.8
|
13.8
|
1.0
|
CG
|
T:ASP46
|
3.9
|
25.3
|
1.0
|
CE1
|
T:TYR44
|
4.0
|
17.1
|
1.0
|
CD
|
T:LYS98
|
4.0
|
19.7
|
1.0
|
CA
|
T:HIS13
|
4.1
|
12.0
|
1.0
|
OD1
|
T:ASP46
|
4.2
|
22.4
|
1.0
|
CB
|
T:HIS13
|
4.2
|
13.1
|
1.0
|
C
|
T:HIS13
|
4.3
|
13.2
|
1.0
|
OH
|
T:TYR44
|
4.5
|
19.7
|
1.0
|
CD2
|
T:HIS13
|
4.5
|
12.9
|
1.0
|
O
|
T:TRP11
|
4.6
|
15.5
|
1.0
|
CE1
|
T:PHE95
|
4.7
|
15.4
|
1.0
|
N
|
T:ILE12
|
4.7
|
13.1
|
1.0
|
CZ
|
T:TYR44
|
4.8
|
18.7
|
1.0
|
CG1
|
T:ILE12
|
4.8
|
13.6
|
1.0
|
CG
|
T:HIS13
|
4.8
|
14.0
|
1.0
|
CD1
|
T:TYR44
|
4.9
|
16.0
|
1.0
|
CB
|
T:ASP46
|
5.0
|
19.2
|
1.0
|
O
|
T:ILE12
|
5.0
|
12.6
|
1.0
|
|
Reference:
S.B.Carr,
W.Li,
K.L.Wong,
R.M.Evans,
S.E.T.Kendall-Price,
P.A.Ash,
K.A.Vincent.
Glutamate Flick Enables Proton Tunnelling During Fast Redox Biocatalysis To Be Published.
Page generated: Sun Jul 13 16:34:20 2025
|