Copper in PDB 6xlt: The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7

Enzymatic activity of The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7

All present enzymatic activity of The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7:
1.1.3.9;

Protein crystallography data

The structure of The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7, PDB code: 6xlt 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)*	28.46 / 1.48
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	97.282, 89.12, 86.162, 90, 117.82, 90
*R / R_free (%)*	14.8 / 16.9

Other elements in 6xlt:

The structure of The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7 also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

Copper Binding Sites:

The binding sites of Copper atom in the The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7 (pdb code 6xlt). 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 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7, PDB code: 6xlt:

Copper binding site 1 out of 1 in 6xlt

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Copper Binding Sites List in 6xlt

Copper binding site 1 out of 1 in the The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7

Mono view

Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu1001 b:20.0 occ:0.54	OH	A:TYR272	1.9	18.0	1.0
	NE2	A:HIS496	2.0	16.5	1.0
	NE2	A:HIS581	2.1	17.1	1.0
	O	A:HOH1169	2.5	31.2	1.0
	OH	A:TYR495	2.8	26.2	1.0
	CE1	A:HIS496	2.9	19.9	1.0
	CZ	A:TYR272	2.9	16.4	1.0
	CD2	A:HIS496	3.0	19.1	1.0
	CD2	A:HIS581	3.1	15.1	1.0
	CE1	A:HIS581	3.2	17.3	1.0
	CZ	A:TYR495	3.3	18.9	1.0
	CE2	A:TYR495	3.4	20.3	1.0
	SG	A:CYS228	3.4	17.6	1.0
	CZ	A:PHE227	3.5	17.1	1.0
	CE1	A:TYR272	3.5	15.6	1.0
	CE2	A:TYR272	3.8	16.3	1.0
	ND1	A:HIS496	4.0	19.7	1.0
	CG	A:HIS496	4.1	17.6	1.0
	CE1	A:PHE227	4.1	18.1	1.0
	CG	A:HIS581	4.2	14.7	1.0
	ND1	A:HIS581	4.2	16.3	1.0
	CE2	A:PHE227	4.2	16.6	1.0
	CE1	A:TYR495	4.4	22.9	1.0
	CD2	A:TYR495	4.6	18.9	1.0
	O	A:HOH1605	4.7	32.4	1.0
	CD1	A:TYR272	4.8	17.4	1.0
	OH	A:TYR405	5.0	17.8	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 07:30:18 2025

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