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Iron 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 (Cl) 3 atoms

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 6bpw

Go 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

A full contact list of Iron with other atoms in the Fe 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:Fe301

b:39.7
occ:1.00
 NE2 A:HIS86 2.3 42.6 1.0
NE2 A:HIS88 2.4 37.0 1.0
NE2 A:HIS140 2.4 42.0 1.0
O A:HOH405 2.6 40.6 1.0
O A:HOH402 2.6 40.1 1.0
O A:HOH475 2.7 39.9 1.0
CD2 A:HIS86 3.1 38.4 1.0
CD2 A:HIS88 3.2 39.0 1.0
CD2 A:HIS140 3.3 38.1 1.0
CE1 A:HIS86 3.3 46.3 1.0
CE1 A:HIS140 3.4 35.6 1.0
CE1 A:HIS88 3.4 44.4 1.0
OH A:2LT157 3.5 40.2 0.7
OH A:2LT157 3.5 38.3 0.3
O A:HOH478 4.1 50.5 1.0
CG A:HIS86 4.3 42.1 1.0
SG A:CYS93 4.4 31.5 0.3
ND1 A:HIS86 4.4 46.0 1.0
CG A:HIS88 4.4 46.2 1.0
CG A:HIS140 4.4 36.1 1.0
O A:HOH439 4.4 52.3 1.0
O A:HOH421 4.5 45.4 1.0
ND1 A:HIS140 4.5 37.6 1.0
ND1 A:HIS88 4.5 53.1 1.0
O A:HOH465 4.5 52.9 1.0
CZ A:2LT157 4.6 36.2 0.3
CZ A:2LT157 4.6 36.0 0.7
CE1 A:2LT157 4.9 36.9 0.3

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: Tue Aug 6 14:37:44 2024

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