Manganese in PDB 2ete: Recombinant Oxalate Oxidase in Complex with Glycolate

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

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

Resolution Low / High (Å)	30.00 / 1.75
Space group	F 4 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	250.434, 250.434, 250.434, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 19.4

The binding sites of Manganese atom in the Recombinant Oxalate Oxidase in Complex with Glycolate (pdb code 2ete). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Recombinant Oxalate Oxidase in Complex with Glycolate, PDB code: 2ete:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Recombinant Oxalate Oxidase in Complex with Glycolate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Recombinant Oxalate Oxidase in Complex with Glycolate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn202 b:10.2 occ:1.00 NE2 A:HIS90 2.1 8.8 1.0 OE1 A:GLU95 2.1 13.2 1.0 NE2 A:HIS137 2.1 12.5 1.0 NE2 A:HIS88 2.3 11.9 1.0 O3 A:GLV404 2.3 29.4 1.0 CD2 A:HIS90 3.0 9.9 1.0 CE1 A:HIS90 3.1 10.5 1.0 CE1 A:HIS137 3.1 11.8 1.0 CD A:GLU95 3.1 13.0 1.0 CD2 A:HIS137 3.1 11.9 1.0 CD2 A:HIS88 3.2 11.4 1.0 CE1 A:HIS88 3.2 12.0 1.0 C2 A:GLV404 3.3 30.1 1.0 OE2 A:GLU95 3.5 14.8 1.0 O2 A:GLV404 3.6 30.3 1.0 ND1 A:HIS90 4.2 10.0 1.0 CG A:HIS90 4.2 10.1 1.0 ND1 A:HIS137 4.2 12.1 1.0 CG A:HIS137 4.3 11.2 1.0 CG A:HIS88 4.3 11.4 1.0 ND1 A:HIS88 4.3 11.7 1.0 CG A:GLU95 4.5 12.3 1.0 C1 A:GLV404 4.6 31.2 1.0 NE2 A:GLN139 4.7 14.4 1.0 CE2 A:PHE153 4.7 9.9 1.0 CB A:GLU95 4.8 11.5 1.0 O1 A:GLV404 4.8 31.5 1.0 CZ A:PHE153 4.9 10.0 1.0

Manganese binding site 2 out of 2 in the Recombinant Oxalate Oxidase in Complex with Glycolate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Recombinant Oxalate Oxidase in Complex with Glycolate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn202 b:9.8 occ:1.00 NE2 B:HIS90 2.1 9.6 1.0 OE1 B:GLU95 2.1 11.8 1.0 NE2 B:HIS137 2.1 11.3 1.0 NE2 B:HIS88 2.3 10.7 1.0 O3 B:GLV406 2.3 33.9 1.0 CD2 B:HIS90 3.0 10.0 1.0 CD2 B:HIS137 3.1 11.0 1.0 CE1 B:HIS137 3.1 10.1 1.0 CE1 B:HIS90 3.1 10.8 1.0 CD B:GLU95 3.1 12.1 1.0 CD2 B:HIS88 3.2 10.8 1.0 CE1 B:HIS88 3.2 11.2 1.0 C2 B:GLV406 3.4 34.3 1.0 OE2 B:GLU95 3.5 14.7 1.0 O2 B:GLV406 3.7 34.9 1.0 CG B:HIS90 4.2 10.1 1.0 ND1 B:HIS90 4.2 10.1 1.0 ND1 B:HIS137 4.2 9.8 1.0 CG B:HIS137 4.2 10.1 1.0 ND1 B:HIS88 4.3 10.6 1.0 CG B:HIS88 4.3 10.7 1.0 CG B:GLU95 4.5 11.6 1.0 C1 B:GLV406 4.5 35.2 1.0 NE2 B:GLN139 4.6 13.4 1.0 CE2 B:PHE153 4.7 10.6 1.0 CB B:GLU95 4.8 11.2 1.0 O1 B:GLV406 4.8 35.7 1.0 CZ B:PHE153 5.0 10.8 1.0

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