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Atomistry » Manganese » PDB 2qjc-2v3y » 2uy9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 2qjc-2v3y » 2uy9 » |
Manganese in PDB 2uy9: E162A Mutant of Bacillus Subtilis Oxalate Decarboxylase OxdcEnzymatic activity of E162A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc
All present enzymatic activity of E162A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc:
4.1.1.2; Protein crystallography data
The structure of E162A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc, PDB code: 2uy9
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:
Manganese Binding Sites:
The binding sites of Manganese atom in the E162A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc
(pdb code 2uy9). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the E162A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc, PDB code: 2uy9: Jump to Manganese binding site number: 1; 2; Manganese binding site 1 out of 2 in 2uy9Go back to Manganese Binding Sites List in 2uy9
Manganese binding site 1 out
of 2 in the E162A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc
Mono view Stereo pair view
Manganese binding site 2 out of 2 in 2uy9Go back to Manganese Binding Sites List in 2uy9
Manganese binding site 2 out
of 2 in the E162A Mutant of Bacillus Subtilis Oxalate Decarboxylase Oxdc
Mono view Stereo pair view
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.
Page generated: Tue Dec 15 04:05:33 2020
ISSN: ISSN 0264-6021 PubMed: 17680775 DOI: 10.1042/BJ20070708 |
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