Manganese in PDB 1uw8: Crystal Structure of Oxalate Decarboxylase

All present enzymatic activity of Crystal Structure of Oxalate Decarboxylase:
4.1.1.2;

The structure of Crystal Structure of Oxalate Decarboxylase, PDB code: 1uw8 was solved by V.J.Just, C.E.M.Stevenson, L.Bowater, A.Tanner, D.M.Lawson, S.Bornemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	91.29 / 2.00
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	154.663, 154.663, 122.822, 90.00, 90.00, 120.00
R / Rfree (%)	12.7 / 15.8

The binding sites of Manganese atom in the Crystal Structure of Oxalate Decarboxylase (pdb code 1uw8). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Oxalate Decarboxylase, PDB code: 1uw8:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Oxalate Decarboxylase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Oxalate Decarboxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1383 b:15.8 occ:1.00 OE1 A:GLU101 2.1 13.0 1.0 NE2 A:HIS95 2.2 13.3 1.0 NE2 A:HIS140 2.3 15.2 1.0 NE2 A:HIS97 2.3 14.4 1.0 O A:HOH2397 2.3 17.5 1.0 O A:HOH2398 2.3 13.9 1.0 CD A:GLU101 3.2 14.9 1.0 CD2 A:HIS95 3.2 14.6 1.0 CE1 A:HIS97 3.2 15.4 1.0 CE1 A:HIS95 3.2 14.8 1.0 CE1 A:HIS140 3.2 16.9 1.0 CD2 A:HIS140 3.3 14.7 1.0 CD2 A:HIS97 3.3 16.8 1.0 OE2 A:GLU101 3.5 15.2 1.0 O A:HOH2210 4.0 24.1 1.0 CE2 A:PHE155 4.3 18.1 1.0 ND1 A:HIS95 4.3 14.3 1.0 ND1 A:HIS97 4.3 15.2 1.0 CG A:HIS95 4.3 13.9 1.0 ND1 A:HIS140 4.4 14.0 1.0 CG A:HIS140 4.4 14.3 1.0 CG A:HIS97 4.4 14.0 1.0 CG A:GLU101 4.5 14.4 1.0 OE2 A:GLU162 4.6 25.3 1.0 CB A:GLU101 4.7 14.7 1.0 CZ A:PHE155 4.7 18.1 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Oxalate Decarboxylase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Oxalate Decarboxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1384 b:16.5 occ:1.00 OE1 A:GLU280 2.1 18.3 1.0 O A:HOH2399 2.2 15.0 1.0 NE2 A:HIS275 2.2 13.6 1.0 NE2 A:HIS319 2.2 15.3 1.0 NE2 A:HIS273 2.3 14.0 1.0 CD2 A:HIS275 3.0 14.3 1.0 CD A:GLU280 3.1 15.4 1.0 CE1 A:HIS273 3.2 15.2 1.0 CE1 A:HIS319 3.2 18.2 1.0 CD2 A:HIS319 3.2 17.3 1.0 CD2 A:HIS273 3.2 14.2 1.0 CE1 A:HIS275 3.3 16.0 1.0 OE2 A:GLU280 3.3 16.5 1.0 OE2 A:GLU333 3.6 21.3 1.0 CD A:GLU333 4.1 21.0 1.0 CG A:HIS275 4.2 14.4 1.0 ND1 A:HIS273 4.3 15.2 1.0 ND1 A:HIS275 4.3 15.5 1.0 ND1 A:HIS319 4.3 15.1 1.0 CG A:HIS273 4.3 14.5 1.0 CG A:HIS319 4.4 15.3 1.0 CG A:GLU280 4.4 13.9 1.0 CG A:GLU333 4.6 16.8 1.0 NH2 A:ARG270 4.6 16.9 1.0 OE1 A:GLU333 4.7 23.5 1.0 CB A:GLU280 4.8 13.9 1.0 CZ A:PHE335 4.8 17.4 1.0 NE A:ARG270 4.9 17.2 1.0

V.J.Just, C.E.M.Stevenson, L.Bowater, A.Tanner, D.M.Lawson, S.Bornemann. A Closed Conformation of Bacillus Subtilis Oxalate Decarboxylase Oxdc Provides Evidence For the True Identity of the Active Site J.Biol.Chem. V. 279 19867 2004.
ISSN: ISSN 0021-9258
PubMed: 14871895
DOI: 10.1074/JBC.M313820200