Chlorine 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 / R_free (%)*	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:

Iron

(Fe)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Cysteine-Bound Ferrous Form of the Matured CL2- TYR157 Human Cysteine Dioxygenase, PDB code: 6bpx:

Chlorine binding site 1 out of 1 in 6bpx

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Chlorine Binding Sites List in 6bpx

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl157 b:60.9 occ:1.00	CL2	A:2LT157	0.0	60.9	1.0
	CE2	A:2LT157	1.7	46.9	1.0
	CZ	A:2LT157	2.6	38.1	1.0
	CD2	A:2LT157	2.7	42.2	1.0
	OH	A:2LT157	3.0	38.5	1.0
	O	A:CYS302	3.1	56.0	1.0
	NH2	A:ARG60	3.3	57.5	1.0
	SD	A:MET73	3.3	49.1	1.0
	C	A:CYS302	3.7	47.3	1.0
	CB	A:HIS155	3.7	32.0	1.0
	ND1	A:HIS155	3.8	36.4	1.0
	CE	A:MET73	3.8	46.2	1.0
	N	A:CYS302	4.0	40.3	1.0
	CE1	A:2LT157	4.0	36.6	1.0
	CG	A:2LT157	4.0	40.1	1.0
	CG	A:HIS155	4.0	35.7	1.0
	CG	A:MET73	4.0	43.9	1.0
	CZ	A:ARG60	4.2	59.1	1.0
	CA	A:CYS302	4.3	48.0	1.0
	CD1	A:LEU75	4.3	31.9	1.0
	OXT	A:CYS302	4.4	49.3	1.0
	NE	A:ARG60	4.5	47.6	1.0
	CD1	A:2LT157	4.5	40.1	1.0
	CB	A:CYS302	4.6	36.3	1.0
	CD2	A:LEU75	4.6	33.6	1.0
	CE1	A:HIS155	4.8	41.2	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 23:00:21 2024

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