› 2zz2

X-ray diffraction
1.53Å resolution

Orotidine Monophosphate Decarboxylase K72A mutant from M. thermoautotrophicum complexed with 6-cyano-UMP

Released:
DOI: 10.2210/pdb2zz2/pdb
PDB entry 2zz2 coloured by chain, front view.
PDB entry 2zz2 coloured by chain, side view.
PDB entry 2zz2 coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus
Primary publication:
Structural characterization of the molecular events during a slow substrate-product transition in orotidine 5'-monophosphate decarboxylase.
Fujihashi M, Wei L, Kotra LP, Pai EF
J Mol Biol 387 1199-210 (2009)
PMID: 19236876

Function and Biology Details

Reaction catalysed: 
Orotidine 5'-phosphate = UMP + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127822 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Orotidine 5'-phosphate decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 252 amino acids
Theoretical weight: 27.32 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O26232 (Residues: 1-228; Coverage: 100%)
Gene names: MTH_129, pyrF
Sequence domains: Orotidine 5'-phosphate decarboxylase / HUMPS family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand 6CN 2 x 6CN
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P21
Unit cell:
a: 58.086Å b: 73.819Å c: 59.323Å
α: 90° β: 119.3° γ: 90°
R-values:
R R work R free
0.161 0.159 0.187
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Specificity in transition state binding: the Pauling model revisited.
Amyes et al. (2013)
1 more

1 mention without citation

Structural characterization of the molecular events during a slow substrate-product transition in orotidine 5'-monophosphate decarboxylase.
Fujihashi et al. (2009)