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Iron in PDB 6bpx: Crystal Structure of Cysteine-Bound Ferrous Form of the Matured CL2- TYR157 Human Cysteine Dioxygenase

Enzymatic activity of Crystal Structure of Cysteine-Bound Ferrous Form of the Matured CL2- TYR157 Human Cysteine Dioxygenase

All present enzymatic activity of Crystal Structure of Cysteine-Bound Ferrous Form of the Matured CL2- TYR157 Human Cysteine Dioxygenase:
1.13.11.20;

Protein crystallography data

The structure of Crystal Structure of Cysteine-Bound Ferrous Form of the Matured CL2- TYR157 Human Cysteine Dioxygenase, PDB code: 6bpx 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) 43.15 / 2.15
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 131.810, 131.810, 34.268, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 21.2

Other elements in 6bpx:

The structure of Crystal Structure of Cysteine-Bound Ferrous Form of the Matured CL2- TYR157 Human Cysteine Dioxygenase also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Cysteine-Bound Ferrous Form of the Matured CL2- TYR157 Human Cysteine Dioxygenase (pdb code 6bpx). 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 Cysteine-Bound Ferrous Form of the Matured CL2- TYR157 Human Cysteine Dioxygenase, PDB code: 6bpx:

Iron binding site 1 out of 1 in 6bpx

Go back to Iron Binding Sites List in 6bpx
Iron binding site 1 out of 1 in the Crystal Structure of Cysteine-Bound Ferrous Form of the Matured CL2- TYR157 Human Cysteine Dioxygenase


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 Cysteine-Bound Ferrous Form of the Matured CL2- TYR157 Human Cysteine Dioxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:35.8
occ:1.00
 NE2 A:HIS86 2.3 35.1 1.0
NE2 A:HIS88 2.3 37.5 1.0
NE2 A:HIS140 2.3 34.1 1.0
O A:HOH413 2.4 38.5 1.0
N A:CYS302 2.5 40.3 1.0
SG A:CYS302 2.5 44.0 1.0
CA A:CYS302 3.1 48.0 1.0
CD2 A:HIS86 3.1 34.7 1.0
CD2 A:HIS88 3.2 34.5 1.0
CD2 A:HIS140 3.3 34.3 1.0
CE1 A:HIS88 3.3 38.5 1.0
CB A:CYS302 3.3 36.3 1.0
CE1 A:HIS140 3.3 35.8 1.0
CE1 A:HIS86 3.3 35.5 1.0
OH A:2LT157 3.8 38.5 1.0
CG A:HIS86 4.3 34.9 1.0
ND1 A:HIS86 4.4 33.4 1.0
ND1 A:HIS88 4.4 41.1 1.0
CG A:HIS88 4.4 36.1 1.0
ND1 A:HIS140 4.4 32.7 1.0
CG A:HIS140 4.4 31.8 1.0
C A:CYS302 4.5 47.3 1.0
SG A:CYS93 4.7 46.2 1.0
CZ A:2LT157 4.9 38.1 1.0
CG2 A:VAL142 4.9 38.0 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: Tue Aug 6 14:37:44 2024

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