Copper in PDB 6xls: The 1.80 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated F2-TYR272

Enzymatic activity of The 1.80 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated F2-TYR272

All present enzymatic activity of The 1.80 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated F2-TYR272:
1.1.3.9;

Protein crystallography data

The structure of The 1.80 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated F2-TYR272, PDB code: 6xls 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)*	41.62 / 1.80
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	97.228, 89.162, 86.159, 90, 117.94, 90
*R / R_free (%)*	14.8 / 18.4

Other elements in 6xls:

The structure of The 1.80 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated F2-TYR272 also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Fluorine	(F)	1 atom

Copper Binding Sites:

The binding sites of Copper atom in the The 1.80 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated F2-TYR272 (pdb code 6xls). 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 1.80 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated F2-TYR272, PDB code: 6xls:

Copper binding site 1 out of 1 in 6xls

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Copper Binding Sites List in 6xls

Copper binding site 1 out of 1 in the The 1.80 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated F2-TYR272

Mono view

Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The 1.80 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated F2-TYR272 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu1001 b:31.7 occ:0.50	OH	A:F2Y272	1.8	27.0	1.0
	OH	A:TYR495	2.1	42.1	1.0
	NE2	A:HIS581	2.2	22.3	1.0
	NE2	A:HIS496	2.3	24.2	1.0
	CZ	A:F2Y272	2.8	22.8	1.0
	CZ	A:TYR495	2.9	28.0	1.0
	CD2	A:HIS581	3.0	26.9	1.0
	O	A:HOH1188	3.0	36.3	1.0
	CE1	A:HIS496	3.2	24.7	1.0
	CD2	A:HIS496	3.2	24.8	1.0
	CE1	A:HIS581	3.3	23.4	1.0
	CE2	A:TYR495	3.4	24.0	1.0
	CE1	A:F2Y272	3.5	21.9	1.0
	SG	A:CYS228	3.6	23.1	1.0
	CE2	A:F2Y272	3.6	26.5	1.0
	F2	A:F2Y272	3.7	27.7	1.0
	CE1	A:TYR495	3.8	27.8	1.0
	CZ	A:PHE227	3.9	19.9	1.0
	CG	A:HIS581	4.2	27.4	1.0
	ND1	A:HIS496	4.3	22.9	1.0
	O	A:HOH1292	4.3	38.8	1.0
	ND1	A:HIS581	4.3	25.9	1.0
	CG	A:HIS496	4.3	23.1	1.0
	OH	A:TYR405	4.5	25.8	1.0
	CE2	A:PHE227	4.5	21.6	1.0
	CE1	A:PHE227	4.6	22.1	1.0
	CD2	A:TYR495	4.6	23.3	1.0
	CD1	A:F2Y272	4.7	23.6	1.0
	CD2	A:F2Y272	4.8	21.9	1.0
	CD1	A:TYR495	4.9	25.9	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: Mon Jul 14 07:30:14 2025

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