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Copper in PDB 2eie: Crystal Structure of Galactose Oxidase Complexed with Azide

Enzymatic activity of Crystal Structure of Galactose Oxidase Complexed with Azide

All present enzymatic activity of Crystal Structure of Galactose Oxidase Complexed with Azide:
1.1.3.9;

Protein crystallography data

The structure of Crystal Structure of Galactose Oxidase Complexed with Azide, PDB code: 2eie 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) 39.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.309, 89.294, 134.370, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 20.9

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Galactose Oxidase Complexed with Azide (pdb code 2eie). 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 Complexed with Azide, PDB code: 2eie:

Copper binding site 1 out of 1 in 2eie

Go back to Copper Binding Sites List in 2eie
Copper binding site 1 out of 1 in the Crystal Structure of Galactose Oxidase Complexed with Azide


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 Complexed with Azide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu700

b:11.4
occ:1.00
OH A:TYR272 1.9 5.2 1.0
NE2 A:HIS496 2.1 6.9 1.0
NE2 A:HIS581 2.1 6.4 1.0
N1 A:AZI2391 2.5 25.9 1.0
CZ A:TYR272 2.8 6.2 1.0
OH A:TYR495 2.9 15.0 1.0
CD2 A:HIS581 3.0 6.2 1.0
CD2 A:HIS496 3.0 9.3 1.0
CE1 A:HIS581 3.2 6.6 1.0
CE1 A:HIS496 3.2 10.0 1.0
SG A:CYS228 3.3 6.7 1.0
CZ A:PHE227 3.3 7.9 1.0
CE1 A:TYR272 3.4 6.3 1.0
CZ A:TYR495 3.4 10.2 1.0
CE2 A:TYR495 3.6 11.4 1.0
N2 A:AZI2391 3.6 26.9 1.0
CE2 A:TYR272 3.9 5.2 1.0
CE1 A:PHE227 4.0 5.7 1.0
CE2 A:PHE227 4.1 7.6 1.0
CG A:HIS581 4.2 4.7 1.0
CG A:HIS496 4.2 6.4 1.0
ND1 A:HIS581 4.2 6.2 1.0
ND1 A:HIS496 4.3 7.3 1.0
CE1 A:TYR495 4.3 11.3 1.0
N3 A:AZI2391 4.5 28.6 1.0
CD2 A:TYR495 4.7 9.6 1.0
CD1 A:TYR272 4.7 6.0 1.0
O A:HOH1225 4.8 19.0 1.0
CB A:CYS228 4.9 6.5 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: Thu Sep 3 16:36:21 2020
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