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Calcium in PDB 2jkx: Galactose Oxidase. Matgo. Copper Free, Expressed in Pichia Pastoris.

Enzymatic activity of Galactose Oxidase. Matgo. Copper Free, Expressed in Pichia Pastoris.

All present enzymatic activity of Galactose Oxidase. Matgo. Copper Free, Expressed in Pichia Pastoris.:
1.1.3.9;

Protein crystallography data

The structure of Galactose Oxidase. Matgo. Copper Free, Expressed in Pichia Pastoris., PDB code: 2jkx was solved by S.E.Deacon, K.Mahmoud, R.K.Spooner, S.J.Firbank, P.F.Knowles, S.E.V.Phillips, M.J.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.24 / 1.84
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 96.950, 88.520, 85.350, 90.00, 117.24, 90.00
R / Rfree (%) 16.3 / 20.1

Calcium Binding Sites:

The binding sites of Calcium atom in the Galactose Oxidase. Matgo. Copper Free, Expressed in Pichia Pastoris. (pdb code 2jkx). 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 Galactose Oxidase. Matgo. Copper Free, Expressed in Pichia Pastoris., PDB code: 2jkx:

Calcium binding site 1 out of 1 in 2jkx

Go back to Calcium Binding Sites List in 2jkx
Calcium binding site 1 out of 1 in the Galactose Oxidase. Matgo. Copper Free, Expressed in Pichia Pastoris.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Galactose Oxidase. Matgo. Copper Free, Expressed in Pichia Pastoris. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1641

b:25.8
occ:1.00
O A:LYS29 2.3 27.2 1.0
O A:THR37 2.3 28.0 1.0
O A:ASN34 2.3 28.0 1.0
OE2 A:GLU142 2.3 24.6 1.0
O A:ALA141 2.4 19.3 1.0
OD1 A:ASP32 2.5 28.4 1.0
OG1 A:THR37 2.5 28.2 1.0
C A:THR37 3.2 29.0 1.0
C A:ASN34 3.4 28.8 1.0
CD A:GLU142 3.5 21.7 1.0
C A:LYS29 3.5 27.6 1.0
CG A:ASP32 3.5 28.8 1.0
C A:ALA141 3.6 20.9 1.0
CB A:THR37 3.7 29.1 1.0
CA A:THR37 3.9 28.9 1.0
OD2 A:ASP32 3.9 29.3 1.0
N A:ASN34 3.9 28.4 1.0
N A:THR37 4.1 29.9 1.0
CA A:ASN34 4.1 28.8 1.0
CG A:GLU142 4.1 20.5 1.0
N A:PHE38 4.2 28.6 1.0
CA A:ALA30 4.3 26.9 1.0
CB A:ASN34 4.3 28.9 1.0
CA A:ALA141 4.3 20.9 1.0
N A:ALA30 4.4 27.1 1.0
OE1 A:GLU142 4.4 22.5 1.0
N A:LYS35 4.5 29.5 1.0
C A:ALA30 4.5 26.6 1.0
CA A:LYS29 4.5 27.9 1.0
N A:ASP32 4.5 26.9 1.0
N A:GLU142 4.6 19.7 1.0
CA A:PHE38 4.6 29.1 1.0
CA A:LYS35 4.7 30.2 1.0
CA A:GLU142 4.8 19.9 1.0
N A:GLY33 4.8 28.0 1.0
CB A:ASP32 4.8 27.9 1.0
CB A:LYS29 4.8 28.4 1.0
N A:ILE31 4.9 26.4 1.0
CG2 A:THR37 4.9 28.6 1.0
CB A:ALA141 4.9 21.5 1.0
O A:ALA30 4.9 26.6 1.0
C A:LYS35 5.0 30.5 1.0

Reference:

S.E.Deacon, K.Mahmoud, R.K.Spooner, S.J.Firbank, P.F.Knowles, S.E.V.Phillips, M.J.Mcpherson. Enhanced Fructose Oxidase Activity in A Galactose Oxidase Variant Chembiochem V. 5 972 2004.
ISSN: ISSN 1439-4227
PubMed: 15239055
DOI: 10.1002/CBIC.200300810
Page generated: Sat Dec 12 03:42:21 2020

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