Fluorine in PDB 6bpv: Crystal Structure of Cysteine-Bound Ferrous Form of the Matured F2- TYR157 Human Cysteine Dioxygenase

Enzymatic activity of Crystal Structure of Cysteine-Bound Ferrous Form of the Matured F2- TYR157 Human Cysteine Dioxygenase

All present enzymatic activity of Crystal Structure of Cysteine-Bound Ferrous Form of the Matured F2- TYR157 Human Cysteine Dioxygenase:
1.13.11.20;

Protein crystallography data

The structure of Crystal Structure of Cysteine-Bound Ferrous Form of the Matured F2- TYR157 Human Cysteine Dioxygenase, PDB code: 6bpv 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) 31.57 / 1.95
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 131.435, 131.435, 34.177, 90.00, 90.00, 120.00
R / Rfree (%) 16 / 17.9

Other elements in 6bpv:

The structure of Crystal Structure of Cysteine-Bound Ferrous Form of the Matured F2- TYR157 Human Cysteine Dioxygenase also contains other interesting chemical elements:

Iron (Fe) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Cysteine-Bound Ferrous Form of the Matured F2- TYR157 Human Cysteine Dioxygenase (pdb code 6bpv). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Cysteine-Bound Ferrous Form of the Matured F2- TYR157 Human Cysteine Dioxygenase, PDB code: 6bpv:

Fluorine binding site 1 out of 1 in 6bpv

Go back to Fluorine Binding Sites List in 6bpv
Fluorine binding site 1 out of 1 in the Crystal Structure of Cysteine-Bound Ferrous Form of the Matured F2- TYR157 Human Cysteine Dioxygenase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Cysteine-Bound Ferrous Form of the Matured F2- TYR157 Human Cysteine Dioxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F157

b:40.3
occ:1.00
 F2 A:F2Y157 0.0 40.3 1.0
CE2 A:F2Y157 1.3 31.6 1.0
CZ A:F2Y157 2.3 29.4 1.0
CD2 A:F2Y157 2.4 31.5 1.0
OH A:F2Y157 2.7 34.7 1.0
OXT A:CYS302 3.0 44.9 1.0
SD A:MET73 3.4 35.9 1.0
NH2 A:ARG60 3.4 48.4 1.0
CB A:HIS155 3.5 23.1 1.0
CE1 A:F2Y157 3.6 27.5 1.0
CG A:F2Y157 3.6 29.1 1.0
ND1 A:HIS155 3.8 26.1 1.0
C A:CYS302 3.9 43.9 1.0
CG A:HIS155 3.9 26.2 1.0
CE A:MET73 4.0 34.0 1.0
CG A:MET73 4.1 29.1 1.0
CD1 A:F2Y157 4.1 29.9 1.0
N A:CYS302 4.2 32.0 1.0
O A:HOH450 4.2 39.4 1.0
CZ A:ARG60 4.4 51.2 1.0
CA A:CYS302 4.5 37.3 1.0
CD1 A:LEU75 4.6 23.2 1.0
NE A:ARG60 4.7 38.1 1.0
O A:CYS302 4.7 41.5 1.0
CB A:CYS302 4.8 33.8 1.0
CA A:HIS155 4.9 20.8 1.0
CE1 A:HIS155 4.9 29.4 1.0
CB A:F2Y157 4.9 26.7 1.0
CD2 A:LEU75 4.9 26.5 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: Sun Dec 13 12:45:50 2020

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