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Copper in PDB 2eic: Crystal Structure of Galactose Oxidase Mutant W290F

Enzymatic activity of Crystal Structure of Galactose Oxidase Mutant W290F

All present enzymatic activity of Crystal Structure of Galactose Oxidase Mutant W290F:
1.1.3.9;

Protein crystallography data

The structure of Crystal Structure of Galactose Oxidase Mutant W290F, PDB code: 2eic was solved by N.Akyumani, S.Tamber, S.J.Firbank, P.F.Knowles, S.E.Phillips, M.J.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 97.770, 88.890, 86.190, 90.00, 117.90, 90.00
R / Rfree (%) 17.7 / 23.3

Other elements in 2eic:

The structure of Crystal Structure of Galactose Oxidase Mutant W290F also contains other interesting chemical elements:

Sodium (Na) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Galactose Oxidase Mutant W290F (pdb code 2eic). 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 Mutant W290F, PDB code: 2eic:

Copper binding site 1 out of 1 in 2eic

Go back to Copper Binding Sites List in 2eic
Copper binding site 1 out of 1 in the Crystal Structure of Galactose Oxidase Mutant W290F


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 Mutant W290F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu641

b:18.4
occ:1.00
OH A:TYR272 2.1 13.6 1.0
NE2 A:HIS496 2.2 12.1 1.0
NE2 A:HIS581 2.2 23.1 1.0
OH A:TYR495 2.6 21.7 1.0
CZ A:TYR272 2.9 10.3 1.0
CD2 A:HIS581 3.1 19.4 1.0
CE1 A:HIS496 3.1 10.5 1.0
CD2 A:HIS496 3.2 12.8 1.0
CE1 A:HIS581 3.3 13.7 1.0
CZ A:PHE227 3.3 13.2 1.0
CZ A:TYR495 3.3 16.7 1.0
CE1 A:TYR272 3.4 6.7 1.0
SG A:CYS228 3.5 12.7 1.0
CE2 A:TYR495 3.6 10.3 1.0
CE2 A:TYR272 4.0 9.9 1.0
CE1 A:PHE227 4.0 1.0 1.0
CE2 A:PHE227 4.1 11.5 1.0
ND1 A:HIS496 4.2 16.5 1.0
CG A:HIS581 4.2 22.4 1.0
CG A:HIS496 4.3 16.8 1.0
ND1 A:HIS581 4.3 19.8 1.0
CE1 A:TYR495 4.4 11.6 1.0
O A:HOH804 4.6 3.9 1.0
CD1 A:TYR272 4.7 6.3 1.0
CD2 A:TYR495 4.8 17.2 1.0

Reference:

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
Page generated: Sun Dec 13 11:04:21 2020

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