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Copper in PDB 2wq8: Glycan Labelling Using Engineered Variants of Galactose Oxidase Obtained By Directed Evolution

Enzymatic activity of Glycan Labelling Using Engineered Variants of Galactose Oxidase Obtained By Directed Evolution

All present enzymatic activity of Glycan Labelling Using Engineered Variants of Galactose Oxidase Obtained By Directed Evolution:
1.1.3.9;

Protein crystallography data

The structure of Glycan Labelling Using Engineered Variants of Galactose Oxidase Obtained By Directed Evolution, PDB code: 2wq8 was solved by J.G.Rannes, A.Ioannou, S.C.Willies, C.Behrens, G.J.Grogan, S.L.Flitsch, N.J.Turner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 76.70 / 2.19
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 88.464, 88.464, 410.846, 90.00, 90.00, 120.00
R / Rfree (%) 18.2 / 24.2

Other elements in 2wq8:

The structure of Glycan Labelling Using Engineered Variants of Galactose Oxidase Obtained By Directed Evolution also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Glycan Labelling Using Engineered Variants of Galactose Oxidase Obtained By Directed Evolution (pdb code 2wq8). 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 Glycan Labelling Using Engineered Variants of Galactose Oxidase Obtained By Directed Evolution, PDB code: 2wq8:

Copper binding site 1 out of 1 in 2wq8

Go back to Copper Binding Sites List in 2wq8
Copper binding site 1 out of 1 in the Glycan Labelling Using Engineered Variants of Galactose Oxidase Obtained 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 Glycan Labelling Using Engineered Variants of Galactose Oxidase Obtained By Directed Evolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1640

b:16.0
occ:1.00
 NE2 A:HIS581 2.1 5.4 1.0
NE2 A:HIS496 2.1 9.4 1.0
OH A:TYR272 2.1 9.3 1.0
OH A:TYR495 2.7 15.3 1.0
OXT A:ACY1642 2.8 33.1 1.0
CZ A:TYR272 2.9 9.5 1.0
CD2 A:HIS496 3.0 6.8 1.0
CE1 A:HIS581 3.0 3.4 1.0
CD2 A:HIS581 3.0 5.0 1.0
CE1 A:HIS496 3.1 6.4 1.0
CZ A:TYR495 3.3 9.6 1.0
CZ A:PHE227 3.3 5.0 1.0
SG A:CYS228 3.4 11.6 1.0
CE1 A:TYR272 3.5 7.1 1.0
CE2 A:TYR495 3.6 13.0 1.0
C A:ACY1642 3.7 32.6 1.0
O A:ACY1642 3.8 32.2 1.0
CE2 A:TYR272 3.9 7.3 1.0
CE1 A:PHE227 4.0 5.8 1.0
CE2 A:PHE227 4.1 5.8 1.0
ND1 A:HIS581 4.1 5.5 1.0
CG A:HIS496 4.2 8.3 1.0
CG A:HIS581 4.2 8.1 1.0
ND1 A:HIS496 4.2 10.7 1.0
CE1 A:TYR495 4.2 9.9 1.0
CD1 A:TYR272 4.7 5.8 1.0
OH A:TYR405 4.8 7.6 1.0
CD2 A:TYR495 4.8 6.7 1.0
CD2 A:TYR272 5.0 8.3 1.0

Reference:

J.B.Rannes, A.Ioannou, S.C.Willies, G.Grogan, C.Behrens, S.L.Flitsch, N.J.Turner. Glycoprotein Labeling Using Engineered Variants of Galactose Oxidase Obtained By Directed Evolution. J.Am.Chem.Soc. V. 133 8436 2011.
ISSN: ISSN 0002-7863
PubMed: 21526835
DOI: 10.1021/JA2018477
Page generated: Wed Jul 31 00:07:14 2024

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