Manganese in PDB 2uya: DEL162-163 Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc

All present enzymatic activity of DEL162-163 Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc:
4.1.1.2;

The structure of DEL162-163 Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc, PDB code: 2uya 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)	58.93 / 2.00
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	154.857, 154.857, 123.274, 90.00, 90.00, 120.00
R / Rfree (%)	12.9 / 16.6

The structure of DEL162-163 Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the DEL162-163 Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc (pdb code 2uya). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the DEL162-163 Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc, PDB code: 2uya:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the DEL162-163 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 DEL162-163 Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1383 b:11.1 occ:1.00 OE1 A:GLU101 2.1 12.0 1.0 NE2 A:HIS95 2.3 10.8 1.0 NE2 A:HIS140 2.3 10.0 1.0 O A:HOH2406 2.3 14.9 1.0 NE2 A:HIS97 2.3 9.9 1.0 O A:HOH2405 2.4 10.4 1.0 CD A:GLU101 3.1 12.9 1.0 CE1 A:HIS95 3.2 11.1 1.0 CE1 A:HIS140 3.3 11.0 1.0 CD2 A:HIS140 3.3 10.2 1.0 CD2 A:HIS95 3.3 10.4 1.0 CD2 A:HIS97 3.3 12.5 1.0 CE1 A:HIS97 3.3 11.2 1.0 OE2 A:GLU101 3.5 13.8 1.0 O A:HOH2149 4.1 26.6 1.0 ND1 A:HIS95 4.3 9.4 1.0 CE2 A:PHE155 4.4 15.1 1.0 ND1 A:HIS140 4.4 8.4 1.0 CG A:HIS95 4.4 10.9 1.0 CG A:HIS140 4.4 9.3 1.0 ND1 A:HIS97 4.4 11.2 1.0 CG A:HIS97 4.4 10.1 1.0 CG A:GLU101 4.5 12.4 1.0 CB A:GLU101 4.7 12.0 1.0 CL A:CL1387 4.8 29.6 1.0 CZ A:PHE155 4.8 15.3 1.0

Manganese binding site 2 out of 2 in the DEL162-163 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 DEL162-163 Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1384 b:13.7 occ:1.00 OE1 A:GLU280 2.1 21.9 1.0 O A:HOH2407 2.2 15.0 1.0 NE2 A:HIS275 2.2 9.2 1.0 NE2 A:HIS319 2.3 11.8 1.0 NE2 A:HIS273 2.3 12.6 1.0 CD A:GLU280 3.0 13.7 1.0 CD2 A:HIS275 3.1 10.3 1.0 CE1 A:HIS273 3.2 11.7 1.0 CE1 A:HIS319 3.2 11.7 1.0 CE1 A:HIS275 3.3 11.4 1.0 CD2 A:HIS319 3.3 9.2 1.0 OE2 A:GLU280 3.3 19.4 1.0 CD2 A:HIS273 3.3 11.7 1.0 OE2 A:GLU333 3.5 26.0 1.0 CD A:GLU333 3.9 21.2 1.0 CG A:HIS275 4.3 8.7 1.0 ND1 A:HIS275 4.3 10.9 1.0 ND1 A:HIS273 4.3 12.4 1.0 ND1 A:HIS319 4.4 10.9 1.0 CG A:GLU280 4.4 12.2 1.0 CG A:HIS319 4.4 9.7 1.0 CG A:HIS273 4.4 11.4 1.0 OE1 A:GLU333 4.5 30.3 1.0 NH2 A:ARG270 4.6 18.1 1.0 CG A:GLU333 4.6 18.2 1.0 CZ A:PHE335 4.8 11.3 1.0 CB A:GLU280 4.8 11.2 1.0 NE A:ARG270 4.9 18.7 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