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Atomistry » Iron » PDB 6bpt-6cd3 » 6bpw » |
Iron in PDB 6bpw: Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked CofactorEnzymatic 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:
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:
Iron Binding Sites:
The binding sites of Iron 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 Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Ferrous Form of the CL2-TYR157 Human Cysteine Dioxygenase with Both Uncrosslinked and Crosslinked Cofactor, PDB code: 6bpw: Iron binding site 1 out of 1 in 6bpwGo back to Iron Binding Sites List in 6bpw
Iron binding site 1 out
of 1 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
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.
Page generated: Sun Dec 13 16:21:44 2020
ISSN: ESSN 1552-4469 PubMed: 29942080 DOI: 10.1038/S41589-018-0085-5 |
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