Manganese in PDB 2uy8: R92A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc

All present enzymatic activity of R92A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc:
4.1.1.2;

The structure of R92A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc, PDB code: 2uy8 was solved by V.J.Just, M.R.Burrell, L.Bowater, I.Mcrobbie, C.E.M.Stevenson, D.M.Lawson, S.Bornemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.12 / 2.80
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	154.486, 154.486, 122.301, 90.00, 90.00, 120.00
R / Rfree (%)	13.4 / 21.1

The binding sites of Manganese atom in the R92A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc (pdb code 2uy8). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the R92A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc, PDB code: 2uy8:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the R92A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of R92A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1383 b:15.7 occ:1.00 NE2 A:HIS97 2.0 12.1 1.0 OE1 A:GLU101 2.0 13.6 1.0 O A:HOH2213 2.1 16.6 1.0 NE2 A:HIS95 2.2 11.9 1.0 NE2 A:HIS140 2.2 11.1 1.0 O A:HOH2214 2.5 27.0 1.0 CE1 A:HIS97 2.9 12.5 1.0 CD2 A:HIS97 3.0 11.0 1.0 CD A:GLU101 3.1 11.3 1.0 CE1 A:HIS95 3.1 12.2 1.0 CE1 A:HIS140 3.2 9.5 1.0 CD2 A:HIS140 3.2 11.2 1.0 CD2 A:HIS95 3.3 11.5 1.0 OE2 A:GLU101 3.4 11.9 1.0 ND1 A:HIS97 4.1 11.9 1.0 CG A:HIS97 4.1 10.6 1.0 ND1 A:HIS95 4.3 12.7 1.0 CE2 A:PHE155 4.3 12.7 1.0 ND1 A:HIS140 4.3 11.5 1.0 CG A:HIS140 4.4 11.5 1.0 CG A:HIS95 4.4 10.9 1.0 CG A:GLU101 4.4 8.1 1.0 CZ A:PHE155 4.4 12.8 1.0 CB A:GLU101 4.7 7.7 1.0

Manganese binding site 2 out of 2 in the R92A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of R92A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1384 b:16.4 occ:1.00 OE1 A:GLU280 2.1 17.0 1.0 NE2 A:HIS275 2.1 15.4 1.0 O A:HOH2215 2.1 21.2 1.0 NE2 A:HIS319 2.3 10.3 1.0 NE2 A:HIS273 2.3 10.9 1.0 CD2 A:HIS275 3.0 14.0 1.0 CE1 A:HIS275 3.1 12.6 1.0 CD A:GLU280 3.2 13.5 1.0 CE1 A:HIS319 3.2 11.0 1.0 CD2 A:HIS319 3.3 9.0 1.0 CD2 A:HIS273 3.3 12.5 1.0 CE1 A:HIS273 3.3 13.0 1.0 OE2 A:GLU333 3.3 17.4 1.0 OE2 A:GLU280 3.6 16.5 1.0 CD A:GLU333 4.0 15.3 1.0 ND1 A:HIS275 4.2 12.4 1.0 CG A:HIS275 4.2 12.7 1.0 ND1 A:HIS319 4.3 10.6 1.0 CG A:HIS319 4.4 10.3 1.0 ND1 A:HIS273 4.4 12.9 1.0 CG A:HIS273 4.4 11.1 1.0 CZ A:PHE335 4.4 10.2 1.0 OE1 A:GLU333 4.5 21.4 1.0 CG A:GLU280 4.5 11.3 1.0 CB A:GLU280 4.8 10.3 1.0 NH2 A:ARG270 4.8 13.5 1.0 CG A:GLU333 4.8 13.8 1.0 NE A:ARG270 4.9 15.9 1.0 CE1 A:PHE335 4.9 7.3 1.0

V.J.Just, M.R.Burrell, L.Bowater, I.Mcrobbie, C.E.M.Stevenson, D.M.Lawson, S.Bornemann. The Identity of the Active Site of Oxalate Decarboxylase and the Importance of the Stability of Active-Site Lid Conformations. Biochem.J. V. 407 397 2007.
ISSN: ISSN 0264-6021
PubMed: 17680775
DOI: 10.1042/BJ20070708