› 1km0

X-ray diffraction
1.7Å resolution

Crystal structure of orotidine monophosphate decarboxylase mutant D70N complexed with 6-azaUMP

Released:
DOI: 10.2210/pdb1km0/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1km0 coloured by chain, front view.
PDB entry 1km0 coloured by chain, side view.
PDB entry 1km0 coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus
Primary publication:
Mapping the active site-ligand interactions of orotidine 5'-monophosphate decarboxylase by crystallography.
Wu N, Gillon W, Pai EF
Biochemistry 41 4002-11 (2002)
PMID: 11900543

Function and Biology Details

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

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 247 amino acids
Theoretical weight: 26.79 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

1 bound ligand:
Ligand UP6 4 x UP6
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P1
Unit cell:
a: 59.761Å b: 59.869Å c: 73.878Å
α: 97.27° β: 100.13° γ: 106.93°
R-values:
R R work R free
0.179 0.179 0.21
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Mechanisms and free energies of enzymatic reactions.
Gao et al. (2006)
4 more

2 mentions without citation

A unified genetic, computational and experimental framework identifies functionally relevant residues of the homing endonuclease I-BmoI.
Kleinstiver et al. (2010)
1 more