Copper in PDB 2eid: Galactose Oxidase W290G Mutant

All present enzymatic activity of Galactose Oxidase W290G Mutant:
1.1.3.9;

The structure of Galactose Oxidase W290G Mutant, PDB code: 2eid was solved by S.E.Phillips, M.J.Mcpherson, P.F.Knowles, N.Akyumani, S.J.Firbank, S.Tamber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.20
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	89.884, 89.884, 415.325, 90.00, 90.00, 120.00
R / Rfree (%)	19.2 / 22.6

The binding sites of Copper atom in the Galactose Oxidase W290G Mutant (pdb code 2eid). 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 Galactose Oxidase W290G Mutant, PDB code: 2eid:

Copper binding site 1 out of 1 in the Galactose Oxidase W290G Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Galactose Oxidase W290G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu640 b:16.7 occ:1.00 OH A:TYR272 2.0 15.0 1.0 NE2 A:HIS496 2.3 8.5 1.0 NE2 A:HIS581 2.4 15.3 1.0 OH A:TYR495 2.8 19.1 1.0 CZ A:TYR272 2.9 17.2 1.0 CD2 A:HIS581 3.0 14.7 1.0 CD2 A:HIS496 3.2 9.1 1.0 CZ A:PHE227 3.3 8.7 1.0 SG A:CYS228 3.3 19.1 1.0 CE1 A:HIS496 3.3 11.2 1.0 CZ A:TYR495 3.4 15.3 1.0 CE1 A:TYR272 3.5 17.0 1.0 CE1 A:HIS581 3.6 14.3 1.0 CE2 A:TYR495 3.9 14.2 1.0 CE1 A:PHE227 3.9 8.1 1.0 CE2 A:TYR272 3.9 17.3 1.0 CE2 A:PHE227 4.1 8.8 1.0 CG A:HIS581 4.2 12.3 1.0 CE1 A:TYR495 4.3 13.2 1.0 CG A:HIS496 4.4 9.2 1.0 ND1 A:HIS496 4.4 9.8 1.0 ND1 A:HIS581 4.5 13.1 1.0 O A:HOH993 4.7 13.0 1.0 CD1 A:TYR272 4.7 16.0 1.0 OH A:TYR405 5.0 11.5 1.0 CD2 A:TYR495 5.0 11.6 1.0 CB A:CYS228 5.0 15.8 1.0

M.S.Rogers, E.M.Tyler, N.Akyumani, C.R.Kurtis, R.K.Spooner, S.E.Deacon, S.Tamber, S.J.Firbank, K.Mahmoud, P.F.Knowles, S.E.Phillips, M.J.Mcpherson, D.M.Dooley. The Stacking Tryptophan of Galactose Oxidase: A Second-Coordination Sphere Residue That Has Profound Effects on Tyrosyl Radical Behavior and Enzyme Catalysis Biochemistry V. 46 4606 2007.
ISSN: ISSN 0006-2960
PubMed: 17385891
DOI: 10.1021/BI062139D