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Manganese in PDB 2uyb: S161A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc

Enzymatic activity of S161A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc

All present enzymatic activity of S161A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc:
4.1.1.2;

Protein crystallography data

The structure of S161A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc, PDB code: 2uyb 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) 30.18 / 2.10
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 154.652, 154.652, 121.892, 90.00, 90.00, 120.00
R / Rfree (%) 13.8 / 18.3

Manganese Binding Sites:

The binding sites of Manganese atom in the S161A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc (pdb code 2uyb). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the S161A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc, PDB code: 2uyb:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2uyb

Go back to Manganese Binding Sites List in 2uyb
Manganese binding site 1 out of 2 in the S161A 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 S161A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1383

b:10.6
occ:1.00
OE1 A:GLU101 2.1 10.0 1.0
NE2 A:HIS95 2.2 8.9 1.0
NE2 A:HIS140 2.3 7.6 1.0
NE2 A:HIS97 2.3 9.7 1.0
O1 A:FMT550 2.3 17.8 1.0
O A:HOH2408 2.5 8.6 1.0
CE1 A:HIS97 3.1 7.9 1.0
CD A:GLU101 3.1 9.8 1.0
CE1 A:HIS95 3.1 7.4 1.0
CD2 A:HIS140 3.2 6.8 1.0
CD2 A:HIS95 3.2 6.7 1.0
CE1 A:HIS140 3.3 8.5 1.0
CD2 A:HIS97 3.4 9.2 1.0
C A:FMT550 3.4 20.4 1.0
OE2 A:GLU101 3.5 12.0 1.0
ND1 A:HIS95 4.3 7.1 1.0
ND1 A:HIS97 4.3 10.0 1.0
O A:HOH2207 4.3 22.4 1.0
CG A:HIS95 4.3 7.4 1.0
ND1 A:HIS140 4.4 6.9 1.0
CE2 A:PHE155 4.4 11.0 1.0
CG A:HIS140 4.4 7.5 1.0
O2 A:FMT550 4.4 19.8 1.0
CG A:GLU101 4.4 9.3 1.0
CG A:HIS97 4.5 9.1 1.0
CB A:GLU101 4.7 8.0 1.0
CZ A:PHE155 4.9 8.3 1.0

Manganese binding site 2 out of 2 in 2uyb

Go back to Manganese Binding Sites List in 2uyb
Manganese binding site 2 out of 2 in the S161A 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 S161A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1384

b:11.5
occ:1.00
OE1 A:GLU280 2.1 15.4 1.0
NE2 A:HIS275 2.1 6.2 1.0
NE2 A:HIS319 2.3 7.8 1.0
O A:HOH2409 2.3 10.3 1.0
NE2 A:HIS273 2.3 6.8 1.0
CD2 A:HIS275 3.0 4.3 1.0
CD A:GLU280 3.1 8.8 1.0
CE1 A:HIS275 3.2 6.8 1.0
CE1 A:HIS273 3.2 7.1 1.0
CE1 A:HIS319 3.2 9.3 1.0
CD2 A:HIS319 3.3 6.6 1.0
CD2 A:HIS273 3.3 5.2 1.0
OE2 A:GLU280 3.4 7.8 1.0
OE2 A:GLU333 3.5 17.7 1.0
CD A:GLU333 4.0 14.7 1.0
CG A:HIS275 4.2 6.0 1.0
ND1 A:HIS275 4.2 6.3 1.0
ND1 A:HIS273 4.3 7.4 1.0
ND1 A:HIS319 4.3 8.2 1.0
CG A:HIS273 4.4 6.0 1.0
CG A:HIS319 4.4 6.8 1.0
CG A:GLU280 4.4 8.4 1.0
OE1 A:GLU333 4.5 17.4 1.0
NH2 A:ARG270 4.6 9.1 1.0
CZ A:PHE335 4.6 9.1 1.0
CG A:GLU333 4.6 12.1 1.0
CB A:GLU280 4.8 7.3 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: Tue Dec 15 04:05:34 2020

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