Copper in PDB 2eib: Crystal Structure of Galactose Oxidase, W290H Mutant

All present enzymatic activity of Crystal Structure of Galactose Oxidase, W290H Mutant:
1.1.3.9;

The structure of Crystal Structure of Galactose Oxidase, W290H Mutant, PDB code: 2eib was solved by S.E.Phillips, M.J.Mcpherson, P.F.Knowles, C.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	98.000, 89.400, 86.700, 90.00, 117.80, 90.00
R / Rfree (%)	n/a / n/a

The structure of Crystal Structure of Galactose Oxidase, W290H Mutant also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Copper atom in the Crystal Structure of Galactose Oxidase, W290H Mutant (pdb code 2eib). 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 Crystal Structure of Galactose Oxidase, W290H Mutant, PDB code: 2eib:

Copper binding site 1 out of 1 in the Crystal Structure of Galactose Oxidase, W290H Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Galactose Oxidase, W290H Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu700 b:35.8 occ:1.00 OH A:TYR272 1.8 20.3 1.0 NE2 A:HIS581 2.2 9.8 1.0 NE2 A:HIS496 2.2 10.4 1.0 OH A:TYR495 2.5 16.0 1.0 O A:ACT703 2.7 32.9 1.0 CZ A:TYR272 2.9 9.4 1.0 CD2 A:HIS581 3.1 5.0 1.0 CE1 A:HIS496 3.1 7.0 1.0 CE1 A:HIS581 3.2 5.6 1.0 OXT A:ACT703 3.3 43.8 1.0 CZ A:TYR495 3.3 22.3 1.0 CD2 A:HIS496 3.3 18.6 1.0 C A:ACT703 3.4 41.2 1.0 CE2 A:TYR495 3.5 29.9 1.0 CZ A:PHE227 3.7 7.8 1.0 CE1 A:TYR272 3.7 10.2 1.0 CE2 A:TYR272 3.8 5.0 1.0 SG A:CYS228 3.8 8.8 1.0 ND1 A:HIS581 4.3 18.6 1.0 CG A:HIS581 4.3 14.5 1.0 ND1 A:HIS496 4.3 15.1 1.0 CE2 A:PHE227 4.3 15.9 1.0 CE1 A:PHE227 4.4 8.9 1.0 CE1 A:TYR495 4.4 18.4 1.0 CG A:HIS496 4.4 11.9 1.0 CD2 A:TYR495 4.7 19.8 1.0 CH3 A:ACT703 4.9 43.8 1.0 CD1 A:TYR272 4.9 5.0 1.0 OH A:TYR405 4.9 9.8 1.0 O A:HOH975 5.0 33.5 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