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Manganese in PDB 2et1: Oxalate Oxidase in Complex with Substrate Analogue Glycolate

Enzymatic activity of Oxalate Oxidase in Complex with Substrate Analogue Glycolate

All present enzymatic activity of Oxalate Oxidase in Complex with Substrate Analogue Glycolate:
1.2.3.4;

Protein crystallography data

The structure of Oxalate Oxidase in Complex with Substrate Analogue Glycolate, PDB code: 2et1 was solved by R.-S.Rose, O.Opaleye, E.-J.Woo, R.W.Pickersgill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.52 / 1.60
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 96.302, 96.302, 108.133, 90.00, 90.00, 120.00
R / Rfree (%) 17.7 / 20.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Oxalate Oxidase in Complex with Substrate Analogue Glycolate (pdb code 2et1). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Oxalate Oxidase in Complex with Substrate Analogue Glycolate, PDB code: 2et1:

Manganese binding site 1 out of 1 in 2et1

Go back to Manganese Binding Sites List in 2et1
Manganese binding site 1 out of 1 in the Oxalate Oxidase in Complex with Substrate Analogue Glycolate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Oxalate Oxidase in Complex with Substrate Analogue Glycolate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn202

b:3.3
occ:1.00
OE1 A:GLU95 2.2 4.0 1.0
NE2 A:HIS90 2.2 3.6 1.0
O3 A:GLV203 2.3 6.0 1.0
O A:HOH221 2.3 5.0 1.0
NE2 A:HIS137 2.3 3.1 1.0
NE2 A:HIS88 2.4 4.4 1.0
CD A:GLU95 3.2 4.8 1.0
C2 A:GLV203 3.2 10.4 1.0
CD2 A:HIS90 3.2 2.5 1.0
CE1 A:HIS90 3.2 4.4 1.0
CD2 A:HIS137 3.3 2.8 1.0
CD2 A:HIS88 3.3 4.2 1.0
CE1 A:HIS137 3.3 2.7 1.0
CE1 A:HIS88 3.3 4.3 1.0
O2 A:GLV203 3.5 11.5 1.0
OE2 A:GLU95 3.5 4.8 1.0
ND1 A:HIS90 4.3 2.3 1.0
CG A:HIS90 4.4 2.0 1.0
ND1 A:HIS137 4.4 2.7 1.0
ND1 A:HIS88 4.4 4.4 1.0
CG A:HIS137 4.4 2.5 1.0
CG A:HIS88 4.4 3.8 1.0
CG A:GLU95 4.5 4.3 1.0
C1 A:GLV203 4.6 12.5 1.0
CE2 A:PHE153 4.6 2.6 1.0
O1 A:GLV203 4.7 15.2 1.0
CZ A:PHE153 4.8 2.5 1.0
NE2 A:GLN139 4.9 7.6 1.0
CB A:GLU95 4.9 4.0 1.0

Reference:

O.Opaleye, R.-S.Rose, M.M.Whittaker, E.-J.Woo, J.W.Whittaker, R.W.Pickersgill. Structural and Spectroscopic Studies Shed Light on the Mechanism of Oxalate Oxidase J.Biol.Chem. V. 281 6428 2006.
ISSN: ISSN 0021-9258
PubMed: 16291738
DOI: 10.1074/JBC.M510256200
Page generated: Tue Dec 15 04:01:24 2020

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