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Chlorine in PDB 6cdh: Crystal Structure of Ferrous Form of the Cl-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor

Enzymatic activity of Crystal Structure of Ferrous Form of the Cl-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor

All present enzymatic activity of Crystal Structure of Ferrous Form of the Cl-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 Cl-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor, PDB code: 6cdh 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) 43.02 / 1.82
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 131.426, 131.426, 34.241, 90.00, 90.00, 120.00
R / Rfree (%) 16.5 / 18.2

Other elements in 6cdh:

The structure of Crystal Structure of Ferrous Form of the Cl-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor also contains other interesting chemical elements:

Iron (Fe) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Ferrous Form of the Cl-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor (pdb code 6cdh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Ferrous Form of the Cl-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor, PDB code: 6cdh:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6cdh

Go back to Chlorine Binding Sites List in 6cdh
Chlorine binding site 1 out of 2 in the Crystal Structure of Ferrous Form of the Cl-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 Cl-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl157

b:39.7
occ:0.40
CL A:3CT157 0.0 39.7 0.4
CE2 A:3CT157 1.7 30.7 0.4
SG A:CYS93 2.0 28.4 0.6
CE1 A:3CT157 2.0 30.4 0.6
CZ A:3CT157 2.1 30.8 0.6
OH A:3CT157 2.2 31.2 0.6
CZ A:3CT157 2.7 32.3 0.4
CD2 A:3CT157 2.7 31.2 0.4
OH A:3CT157 2.9 33.0 0.4
O A:HOH411 3.0 35.8 1.0
CD1 A:3CT157 3.1 30.8 0.6
CE2 A:3CT157 3.2 32.6 0.6
O A:PHE94 3.2 25.1 1.0
ND1 A:HIS155 3.3 30.3 1.0
CB A:CYS93 3.5 28.4 0.4
CB A:CYS93 3.5 28.4 0.6
CB A:HIS155 3.6 27.2 1.0
N A:PHE94 3.7 23.4 1.0
C A:PHE94 3.8 26.6 1.0
C A:CYS93 3.8 25.5 1.0
CA A:CYS93 3.9 25.4 0.6
CG A:HIS155 3.9 31.5 1.0
CA A:CYS93 3.9 25.5 0.4
CG A:3CT157 3.9 29.7 0.6
CD2 A:3CT157 3.9 31.8 0.6
CE1 A:3CT157 4.0 33.9 0.4
CG A:3CT157 4.0 29.8 0.4
O A:LEU156 4.1 25.7 1.0
CA A:HIS155 4.2 23.5 1.0
N A:LEU156 4.2 24.0 1.0
CL A:3CT157 4.2 46.5 0.6
SG A:CYS93 4.3 33.2 0.4
CA A:PHE94 4.4 21.9 1.0
CE1 A:HIS155 4.4 33.4 1.0
N A:LEU95 4.5 22.1 1.0
CD1 A:3CT157 4.5 33.7 0.4
O A:CYS93 4.5 27.9 1.0
C A:HIS155 4.5 24.9 1.0
C A:LEU156 4.5 23.8 1.0
CB A:LEU95 4.6 30.4 1.0
O A:HOH403 4.6 37.5 1.0
CA A:LEU95 4.7 22.8 1.0

Chlorine binding site 2 out of 2 in 6cdh

Go back to Chlorine Binding Sites List in 6cdh
Chlorine binding site 2 out of 2 in the Crystal Structure of Ferrous Form of the Cl-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 Cl-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl157

b:46.5
occ:0.60
CL A:3CT157 0.0 46.5 0.6
CE2 A:3CT157 1.7 32.6 0.6
CE1 A:3CT157 2.1 33.9 0.4
CZ A:3CT157 2.2 32.3 0.4
OH A:3CT157 2.3 33.0 0.4
CZ A:3CT157 2.7 30.8 0.6
CD2 A:3CT157 2.7 31.8 0.6
OH A:3CT157 2.9 31.2 0.6
O A:HOH425 3.0 53.6 1.0
CD1 A:3CT157 3.1 33.7 0.4
NH1 A:ARG60 3.1 41.5 0.5
CE2 A:3CT157 3.2 30.7 0.4
SD A:MET73 3.3 40.6 1.0
CB A:HIS155 3.5 27.2 1.0
ND1 A:HIS155 3.6 30.3 1.0
CG A:HIS155 3.8 31.5 1.0
CG A:3CT157 3.9 29.8 0.4
CD2 A:3CT157 3.9 31.2 0.4
CG A:MET73 3.9 32.3 1.0
CE1 A:3CT157 3.9 30.4 0.6
CG A:3CT157 4.0 29.7 0.6
O A:HOH403 4.1 37.5 1.0
CE A:MET73 4.2 36.0 1.0
CL A:3CT157 4.2 39.7 0.4
CZ A:ARG60 4.4 40.0 0.5
CD1 A:LEU75 4.5 28.0 1.0
CD1 A:3CT157 4.5 30.8 0.6
CE1 A:HIS155 4.6 33.4 1.0
CE A:MET179 4.6 51.4 0.6
CD2 A:HIS155 4.9 27.6 1.0
CD2 A:LEU75 4.9 29.9 1.0
CA A:HIS155 4.9 23.5 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 23:26:57 2024

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