Copper in PDB 1t2x: Glactose Oxidase C383S Mutant Identified By Directed Evolution

Enzymatic activity of Glactose Oxidase C383S Mutant Identified By Directed Evolution

All present enzymatic activity of Glactose Oxidase C383S Mutant Identified By Directed Evolution:
1.1.3.9;

Protein crystallography data

The structure of Glactose Oxidase C383S Mutant Identified By Directed Evolution, PDB code: 1t2x was solved by D.Wilkinson, N.Akumanyi, R.Hurtado-Guerrero, H.Dawkes, P.F.Knowles, S.E.V.Phillips, M.J.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	61.98 / 2.30
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	97.376, 88.995, 85.800, 90.00, 117.49, 90.00
*R / R_free (%)*	21.8 / 22.8

Other elements in 1t2x:

The structure of Glactose Oxidase C383S Mutant Identified By Directed Evolution also contains other interesting chemical elements:

Sodium

(Na)

1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Glactose Oxidase C383S Mutant Identified By Directed Evolution (pdb code 1t2x). 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 Glactose Oxidase C383S Mutant Identified By Directed Evolution, PDB code: 1t2x:

Copper binding site 1 out of 1 in 1t2x

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Copper Binding Sites List in 1t2x

Copper binding site 1 out of 1 in the Glactose Oxidase C383S Mutant Identified By Directed Evolution

Mono view

Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Glactose Oxidase C383S Mutant Identified By Directed Evolution within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cu641 b:30.6 occ:0.90	NE2	A:HIS496	2.0	23.2	1.0
	OH	A:TYR272	2.0	27.9	1.0
	NE2	A:HIS581	2.1	20.4	1.0
	OH	A:TYR495	2.7	28.6	1.0
	CZ	A:TYR272	2.9	24.8	1.0
	CD2	A:HIS496	2.9	21.3	1.0
	CD2	A:HIS581	2.9	19.2	1.0
	CE1	A:HIS496	3.0	20.4	1.0
	CE1	A:HIS581	3.2	21.1	1.0
	CZ	A:TYR495	3.3	26.4	1.0
	O	A:HOH956	3.3	30.4	0.6
	SG	A:CYS228	3.4	24.6	1.0
	CE1	A:TYR272	3.4	22.8	1.0
	CZ	A:PHE227	3.4	22.6	1.0
	CE2	A:TYR495	3.6	24.0	1.0
	CE2	A:TYR272	3.9	22.2	1.0
	CG	A:HIS496	4.1	22.9	1.0
	ND1	A:HIS496	4.1	22.4	1.0
	CE1	A:PHE227	4.1	21.1	1.0
	CG	A:HIS581	4.1	19.5	1.0
	OXT	A:ACT643	4.1	37.5	0.3
	CE2	A:PHE227	4.2	22.5	1.0
	ND1	A:HIS581	4.2	22.6	1.0
	CE1	A:TYR495	4.3	24.2	1.0
	CD2	A:TYR495	4.7	23.0	1.0
	CD1	A:TYR272	4.7	21.7	1.0
	O	A:ACT643	4.8	37.2	0.3
	OH	A:TYR405	4.8	29.1	1.0
	C	A:ACT643	4.8	37.2	0.3

Reference:

D.Wilkinson, N.Akumanyi, R.Hurtado-Guerrero, H.Dawkes, P.F.Knowles, S.E.V.Phillips, M.J.Mcpherson. Structural and Kinetic Studies of A Series of Mutants of Galactose Oxidase Identified By Directed Evolution. Protein Eng.Des.Sel. V. 17 141 2004.
ISSN: ISSN 1741-0126
PubMed: 15047910
DOI: 10.1093/PROTEIN/GZH018

Page generated: Wed Oct 28 14:17:20 2020

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