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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 2uya:

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

Manganese (Mn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the DEL162-163 Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc, PDB code: 2uya:

Chlorine binding site 1 out of 1 in 2uya

Go back to Chlorine Binding Sites List in 2uya
Chlorine binding site 1 out of 1 in the DEL162-163 Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl 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:Cl1387

b:29.6
occ:1.00
 O A:HOH2406 2.8 14.9 1.0
O A:HOH2149 2.9 26.6 1.0
O A:HOH2255 3.0 31.6 1.0
NH2 A:ARG92 3.3 16.2 1.0
NE A:ARG92 3.4 15.7 1.0
CZ A:ARG92 3.8 18.5 1.0
CE A:MET84 3.8 12.3 1.0
OH A:TYR200 4.2 22.7 1.0
CD1 A:LEU153 4.4 15.6 1.0
CG2 A:THR165 4.4 16.5 1.0
CZ A:PHE160 4.4 21.4 1.0
CZ A:PHE155 4.6 15.3 1.0
CE1 A:TYR200 4.6 20.6 1.0
CD A:ARG92 4.6 14.9 1.0
O A:HOH2214 4.7 27.8 1.0
NE2 A:HIS95 4.7 10.8 1.0
O A:HOH2405 4.7 10.4 1.0
MN A:MN1383 4.8 11.1 1.0
CZ A:TYR200 4.8 20.5 1.0
SD A:MET84 5.0 14.2 1.0
CG1 A:VAL82 5.0 9.9 1.0

Reference:

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
Page generated: Fri Jul 11 00:35:21 2025

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