Chlorine in PDB 6bpw: Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor
Enzymatic activity of Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor
All present enzymatic activity of Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor:
1.13.11.20;
Protein crystallography data
The structure of Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor, PDB code: 6bpw
was solved by
A.Liu,
J.Li,
I.Shin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
32.83 /
2.43
|
Space group
|
P 65
|
Cell size a, b, c (Å), α, β, γ (°)
|
131.098,
131.098,
34.292,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
16 /
20.6
|
Other elements in 6bpw:
The structure of Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor
(pdb code 6bpw). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the
Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor, PDB code: 6bpw:
Jump to Chlorine binding site number:
1;
2;
3;
Chlorine binding site 1 out
of 3 in 6bpw
Go back to
Chlorine Binding Sites List in 6bpw
Chlorine binding site 1 out
of 3 in the Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor
 Mono view
 Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl157
b:44.1
occ:0.65
|
CL1
|
A:2LT157
|
0.0
|
44.1
|
0.7
|
CE1
|
A:2LT157
|
1.7
|
36.7
|
0.7
|
CE1
|
A:2LT157
|
2.0
|
36.9
|
0.3
|
CZ
|
A:2LT157
|
2.1
|
36.2
|
0.3
|
SG
|
A:CYS93
|
2.2
|
31.5
|
0.3
|
OH
|
A:2LT157
|
2.4
|
38.3
|
0.3
|
CD1
|
A:2LT157
|
2.7
|
35.5
|
0.7
|
CZ
|
A:2LT157
|
2.7
|
36.0
|
0.7
|
CD1
|
A:2LT157
|
2.9
|
36.0
|
0.3
|
OH
|
A:2LT157
|
3.0
|
40.2
|
0.7
|
O
|
A:HOH405
|
3.1
|
40.6
|
1.0
|
O
|
A:PHE94
|
3.1
|
31.9
|
1.0
|
CE2
|
A:2LT157
|
3.1
|
35.6
|
0.3
|
ND1
|
A:HIS155
|
3.3
|
35.5
|
1.0
|
CB
|
A:CYS93
|
3.5
|
37.1
|
0.7
|
CB
|
A:CYS93
|
3.6
|
37.1
|
0.3
|
CB
|
A:HIS155
|
3.6
|
31.3
|
1.0
|
N
|
A:PHE94
|
3.7
|
32.2
|
1.0
|
C
|
A:PHE94
|
3.7
|
31.6
|
1.0
|
CG
|
A:2LT157
|
3.7
|
34.6
|
0.3
|
CG
|
A:HIS155
|
3.8
|
37.4
|
1.0
|
CD2
|
A:2LT157
|
3.8
|
35.5
|
0.3
|
C
|
A:CYS93
|
3.8
|
33.0
|
1.0
|
CA
|
A:CYS93
|
3.9
|
34.8
|
0.3
|
CA
|
A:CYS93
|
3.9
|
34.8
|
0.7
|
O
|
A:LEU156
|
3.9
|
32.0
|
1.0
|
CG
|
A:2LT157
|
4.0
|
34.2
|
0.7
|
CE2
|
A:2LT157
|
4.0
|
40.9
|
0.7
|
CA
|
A:HIS155
|
4.1
|
32.4
|
1.0
|
N
|
A:LEU156
|
4.1
|
25.2
|
1.0
|
CL2
|
A:2LT157
|
4.2
|
40.4
|
0.3
|
CA
|
A:PHE94
|
4.3
|
27.3
|
1.0
|
CE1
|
A:HIS155
|
4.3
|
41.1
|
1.0
|
CB
|
A:LEU95
|
4.4
|
29.6
|
1.0
|
N
|
A:LEU95
|
4.4
|
29.5
|
1.0
|
SG
|
A:CYS93
|
4.4
|
41.7
|
0.7
|
C
|
A:LEU156
|
4.5
|
30.8
|
1.0
|
C
|
A:HIS155
|
4.5
|
34.7
|
1.0
|
O
|
A:CYS93
|
4.5
|
27.5
|
1.0
|
CD2
|
A:2LT157
|
4.5
|
36.8
|
0.7
|
CA
|
A:LEU95
|
4.6
|
26.3
|
1.0
|
CG
|
A:LEU95
|
4.9
|
39.9
|
1.0
|
O
|
A:HOH402
|
4.9
|
40.1
|
1.0
|
CD2
|
A:HIS155
|
5.0
|
35.4
|
1.0
|
CA
|
A:LEU156
|
5.0
|
28.4
|
1.0
|
|
Chlorine binding site 2 out
of 3 in 6bpw
Go back to
Chlorine Binding Sites List in 6bpw
Chlorine binding site 2 out
of 3 in the Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor
 Mono view
 Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl157
b:47.0
occ:0.65
|
CL2
|
A:2LT157
|
0.0
|
47.0
|
0.7
|
CE2
|
A:2LT157
|
1.7
|
40.9
|
0.7
|
CD2
|
A:2LT157
|
2.7
|
36.8
|
0.7
|
CZ
|
A:2LT157
|
2.7
|
36.0
|
0.7
|
CL2
|
A:2LT157
|
2.7
|
40.4
|
0.3
|
CE2
|
A:2LT157
|
2.8
|
35.6
|
0.3
|
O
|
A:HOH402
|
2.8
|
40.1
|
1.0
|
OH
|
A:2LT157
|
3.0
|
40.2
|
0.7
|
O
|
A:HOH421
|
3.2
|
45.4
|
1.0
|
CD2
|
A:2LT157
|
3.3
|
35.5
|
0.3
|
CZ
|
A:2LT157
|
3.3
|
36.2
|
0.3
|
O
|
A:HOH439
|
3.4
|
52.3
|
1.0
|
SD
|
A:MET179
|
3.4
|
74.2
|
1.0
|
NH1
|
A:ARG60
|
3.6
|
42.9
|
0.7
|
NH1
|
A:ARG60
|
3.7
|
43.3
|
0.3
|
CZ
|
A:PHE161
|
3.8
|
36.2
|
1.0
|
OH
|
A:2LT157
|
3.8
|
38.3
|
0.3
|
O
|
A:HOH465
|
3.8
|
52.9
|
1.0
|
CE
|
A:MET179
|
4.0
|
57.7
|
1.0
|
CG
|
A:2LT157
|
4.0
|
34.2
|
0.7
|
CE1
|
A:2LT157
|
4.1
|
36.7
|
0.7
|
CE1
|
A:PHE161
|
4.1
|
39.0
|
1.0
|
CG
|
A:2LT157
|
4.2
|
34.6
|
0.3
|
CE1
|
A:2LT157
|
4.2
|
36.9
|
0.3
|
NH2
|
A:ARG60
|
4.3
|
45.5
|
0.3
|
O
|
A:HOH401
|
4.4
|
58.6
|
1.0
|
CZ
|
A:ARG60
|
4.4
|
45.5
|
0.3
|
CZ
|
A:ARG60
|
4.5
|
45.3
|
0.7
|
CD1
|
A:2LT157
|
4.5
|
35.5
|
0.7
|
CD1
|
A:2LT157
|
4.6
|
36.0
|
0.3
|
CE2
|
A:PHE161
|
4.6
|
38.8
|
1.0
|
NH2
|
A:ARG60
|
4.9
|
49.0
|
0.7
|
SD
|
A:MET73
|
4.9
|
54.6
|
1.0
|
|
Chlorine binding site 3 out
of 3 in 6bpw
Go back to
Chlorine Binding Sites List in 6bpw
Chlorine binding site 3 out
of 3 in the Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor
 Mono view
 Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl157
b:40.4
occ:0.35
|
CL2
|
A:2LT157
|
0.0
|
40.4
|
0.3
|
CE2
|
A:2LT157
|
1.7
|
35.6
|
0.3
|
CZ
|
A:2LT157
|
2.3
|
36.0
|
0.7
|
CE2
|
A:2LT157
|
2.4
|
40.9
|
0.7
|
OH
|
A:2LT157
|
2.5
|
40.2
|
0.7
|
CZ
|
A:2LT157
|
2.7
|
36.2
|
0.3
|
CD2
|
A:2LT157
|
2.7
|
35.5
|
0.3
|
CL2
|
A:2LT157
|
2.7
|
47.0
|
0.7
|
O
|
A:HOH421
|
2.9
|
45.4
|
1.0
|
OH
|
A:2LT157
|
3.0
|
38.3
|
0.3
|
CE1
|
A:2LT157
|
3.2
|
36.7
|
0.7
|
CD2
|
A:2LT157
|
3.2
|
36.8
|
0.7
|
SD
|
A:MET73
|
3.3
|
54.6
|
1.0
|
NH1
|
A:ARG60
|
3.4
|
42.9
|
0.7
|
ND1
|
A:HIS155
|
3.4
|
35.5
|
1.0
|
CB
|
A:HIS155
|
3.5
|
31.3
|
1.0
|
NH1
|
A:ARG60
|
3.5
|
43.3
|
0.3
|
CG
|
A:HIS155
|
3.7
|
37.4
|
1.0
|
CG
|
A:MET73
|
3.8
|
41.1
|
1.0
|
CD1
|
A:2LT157
|
3.9
|
35.5
|
0.7
|
CG
|
A:2LT157
|
3.9
|
34.2
|
0.7
|
O
|
A:HOH402
|
4.0
|
40.1
|
1.0
|
CG
|
A:2LT157
|
4.0
|
34.6
|
0.3
|
CE1
|
A:2LT157
|
4.0
|
36.9
|
0.3
|
CL1
|
A:2LT157
|
4.2
|
44.1
|
0.7
|
CD1
|
A:LEU75
|
4.3
|
28.5
|
1.0
|
CE
|
A:MET73
|
4.3
|
44.9
|
1.0
|
CE1
|
A:HIS155
|
4.4
|
41.1
|
1.0
|
CD1
|
A:2LT157
|
4.5
|
36.0
|
0.3
|
CZ
|
A:ARG60
|
4.5
|
45.5
|
0.3
|
CZ
|
A:ARG60
|
4.7
|
45.3
|
0.7
|
NH2
|
A:ARG60
|
4.7
|
45.5
|
0.3
|
CD2
|
A:HIS155
|
4.7
|
35.4
|
1.0
|
CD2
|
A:LEU75
|
4.9
|
36.3
|
1.0
|
CA
|
A:HIS155
|
4.9
|
32.4
|
1.0
|
|
Reference:
J.Li,
W.P.Griffith,
I.Davis,
I.Shin,
J.Wang,
F.Li,
Y.Wang,
D.J.Wherritt,
A.Liu.
Cleavage of A Carbon-Fluorine Bond By An Engineered Cysteine Dioxygenase. Nat. Chem. Biol. V. 14 853 2018.
ISSN: ESSN 1552-4469
PubMed: 29942080
DOI: 10.1038/S41589-018-0085-5
Page generated: Fri Jul 26 23:00:05 2024
|