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Copper in PDB 6xlr: The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272

Enzymatic activity of The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272

All present enzymatic activity of The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272:
1.1.3.9;

Protein crystallography data

The structure of The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272, PDB code: 6xlr was solved by A.Liu, J.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.59 / 1.23
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 97.204, 88.977, 85.967, 90, 117.91, 90
R / Rfree (%) 15.5 / 17.2

Other elements in 6xlr:

The structure of The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272 also contains other interesting chemical elements:

Calcium (Ca) 1 atom
Chlorine (Cl) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272 (pdb code 6xlr). 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 The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272, PDB code: 6xlr:

Copper binding site 1 out of 1 in 6xlr

Go back to Copper Binding Sites List in 6xlr
Copper binding site 1 out of 1 in the The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The 1.23 Angstrom Crystal Structure of Galactose Oxidase Variant with Genetically Incorporated CL2-TYR272 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:14.2
occ:0.51
 OH A:2LT272 1.8 12.9 1.0
NE2 A:HIS496 1.9 11.6 1.0
NE2 A:HIS581 2.1 11.6 1.0
OH A:TYR495 2.6 21.4 1.0
CZ A:2LT272 2.9 11.6 1.0
CE1 A:HIS496 2.9 13.2 1.0
O A:HOH1202 2.9 21.1 1.0
CD2 A:HIS496 2.9 12.3 1.0
CD2 A:HIS581 3.0 11.0 1.0
CE1 A:HIS581 3.1 12.4 1.0
CZ A:TYR495 3.2 16.7 1.0
SG A:CYS228 3.3 11.5 1.0
CE1 A:2LT272 3.4 11.3 1.0
CZ A:PHE227 3.5 13.2 1.0
CE2 A:2LT272 3.9 11.6 1.0
CE1 A:TYR495 3.9 14.9 1.0
CE2 A:TYR495 3.9 15.7 1.0
ND1 A:HIS496 4.0 12.4 1.0
CG A:HIS496 4.1 11.9 1.0
CE1 A:PHE227 4.1 12.5 1.0
ND1 A:HIS581 4.2 12.0 1.0
CG A:HIS581 4.2 10.8 1.0
CE2 A:PHE227 4.2 12.7 1.0
CL2 A:2LT272 4.2 15.0 1.0
CD1 A:2LT272 4.7 10.3 1.0
CD2 A:TYR495 4.9 13.6 1.0
CD1 A:TYR495 5.0 14.2 1.0

Reference:

J.Li, I.Davis, W.P.Griffith, A.Liu. Formation of Monofluorinated Radical Cofactor in Galactose Oxidase Through Copper-Mediated C-F Bond Scission. J.Am.Chem.Soc. V. 142 18753 2020.
ISSN: ESSN 1520-5126
PubMed: 33091303
DOI: 10.1021/JACS.0C08992
Page generated: Wed Jul 31 07:49:45 2024

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