Copper in PDB 6xlr: The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272

Enzymatic activity of The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272

All present enzymatic activity of The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272:
1.1.3.9;

Protein crystallography data

The structure of The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272, PDB code: 6xlr was solved by A.Liu, J.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	31.59 / 1.23
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	97.204, 88.977, 85.967, 90, 117.91, 90
*R / R_free (%)*	15.5 / 17.2

Other elements in 6xlr:

The structure of The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272 also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Chlorine	(Cl)	1 atom

Copper Binding Sites:

The binding sites of Copper atom in the The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272 (pdb code 6xlr). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272, PDB code: 6xlr:

Copper binding site 1 out of 1 in 6xlr

Go back to

Copper Binding Sites List in 6xlr

Copper binding site 1 out of 1 in the The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272

Mono view

Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu1001 b:14.2 occ:0.51	OH	A:2LT272	1.8	12.9	1.0
	NE2	A:HIS496	1.9	11.6	1.0
	NE2	A:HIS581	2.1	11.6	1.0
	OH	A:TYR495	2.6	21.4	1.0
	CZ	A:2LT272	2.9	11.6	1.0
	CE1	A:HIS496	2.9	13.2	1.0
	O	A:HOH1202	2.9	21.1	1.0
	CD2	A:HIS496	2.9	12.3	1.0
	CD2	A:HIS581	3.0	11.0	1.0
	CE1	A:HIS581	3.1	12.4	1.0
	CZ	A:TYR495	3.2	16.7	1.0
	SG	A:CYS228	3.3	11.5	1.0
	CE1	A:2LT272	3.4	11.3	1.0
	CZ	A:PHE227	3.5	13.2	1.0
	CE2	A:2LT272	3.9	11.6	1.0
	CE1	A:TYR495	3.9	14.9	1.0
	CE2	A:TYR495	3.9	15.7	1.0
	ND1	A:HIS496	4.0	12.4	1.0
	CG	A:HIS496	4.1	11.9	1.0
	CE1	A:PHE227	4.1	12.5	1.0
	ND1	A:HIS581	4.2	12.0	1.0
	CG	A:HIS581	4.2	10.8	1.0
	CE2	A:PHE227	4.2	12.7	1.0
	CL2	A:2LT272	4.2	15.0	1.0
	CD1	A:2LT272	4.7	10.3	1.0
	CD2	A:TYR495	4.9	13.6	1.0
	CD1	A:TYR495	5.0	14.2	1.0

Reference:

J.Li, I.Davis, W.P.Griffith, A.Liu. Formation of Monofluorinated Radical Cofactor in Galactose Oxidase Through Copper-Mediated C-F Bond Scission. J.Am.Chem.Soc. V. 142 18753 2020.
ISSN: ESSN 1520-5126
PubMed: 33091303
DOI: 10.1021/JACS.0C08992

Page generated: Wed Jul 31 07:49:45 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy