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Calcium in PDB 6xlt: The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7

Enzymatic activity of The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7

All present enzymatic activity of The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7:
1.1.3.9;

Protein crystallography data

The structure of The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7, PDB code: 6xlt 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) 28.46 / 1.48
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 97.282, 89.12, 86.162, 90, 117.82, 90
R / Rfree (%) 14.8 / 16.9

Other elements in 6xlt:

The structure of The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7 also contains other interesting chemical elements:

Copper (Cu) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7 (pdb code 6xlt). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7, PDB code: 6xlt:

Calcium binding site 1 out of 1 in 6xlt

Go back to Calcium Binding Sites List in 6xlt
Calcium binding site 1 out of 1 in the The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The 1.48 Angstrom Crystal Structure of Evolved Galactose Oxidase Variant A3.E7 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1002

b:31.6
occ:0.93
 O A:ASN34 2.2 43.7 1.0
O A:LYS29 2.3 29.3 1.0
OE2 A:GLU142 2.4 34.6 1.0
O A:THR37 2.4 34.5 1.0
O A:ALA141 2.4 31.1 1.0
OG1 A:THR37 2.5 38.6 1.0
OD1 A:ASP32 2.5 38.3 1.0
C A:THR37 3.2 33.8 1.0
C A:ASN34 3.3 40.8 1.0
CD A:GLU142 3.5 33.2 1.0
C A:LYS29 3.5 31.5 1.0
CG A:ASP32 3.5 35.9 1.0
C A:ALA141 3.6 28.2 1.0
CB A:THR37 3.6 40.2 1.0
CA A:THR37 3.8 35.3 1.0
OD2 A:ASP32 3.8 37.8 1.0
N A:ASN34 3.9 42.1 1.0
N A:THR37 3.9 40.0 1.0
CA A:ASN34 3.9 41.2 1.0
CG A:GLU142 4.0 29.3 1.0
CB A:ASN34 4.1 39.6 1.0
N A:PHE38 4.2 31.8 1.0
CA A:ALA141 4.3 26.7 1.0
CA A:ALA30 4.3 27.9 1.0
N A:LYS35 4.4 35.3 1.0
N A:ALA30 4.4 32.2 1.0
CA A:LYS29 4.5 36.8 1.0
OE1 A:GLU142 4.5 36.1 1.0
C A:ALA30 4.6 31.0 1.0
CA A:PHE38 4.6 36.0 1.0
N A:GLU142 4.6 28.4 1.0
N A:ASP32 4.6 36.2 1.0
CA A:LYS35 4.7 38.5 1.0
CG2 A:THR37 4.8 36.6 1.0
CB A:LYS29 4.8 35.9 1.0
C A:LYS35 4.8 41.3 1.0
CA A:GLU142 4.8 26.7 1.0
N A:GLY33 4.8 37.4 1.0
CB A:ALA141 4.8 30.7 1.0
CB A:ASP32 4.8 33.7 1.0
N A:ILE31 4.9 31.8 1.0
C A:GLY33 5.0 45.3 1.0
O A:ALA30 5.0 30.9 1.0
N A:ASP36 5.0 40.0 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: Tue Jul 16 18:04:12 2024

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