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X-ray diffraction
1.1Å resolution

K314A mutant of human orotidyl-5'-monophosphate decarboxylase soaked with OMP, decarboxylated to UMP

Released:
DOI: 10.2210/pdb3ewy/pdb
PDB entry 3ewy coloured by chain, front view.
PDB entry 3ewy coloured by chain, side view.
PDB entry 3ewy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Lys314 is a nucleophile in non-classical reactions of orotidine-5'-monophosphate decarboxylase.
Heinrich D, Diederichsen U, Rudolph MG
Chemistry 15 6619-25 (2009)
PMID: 19472232

Function and Biology Details

Reactions catalysed: 
Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
Orotidine 5'-phosphate = UMP + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145693 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridine 5'-monophosphate synthase Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 28.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11172 (Residues: 224-480; Coverage: 54%)
Gene names: OK/SW-cl.21, UMPS
Sequence domains: Orotidine 5'-phosphate decarboxylase / HUMPS family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand U5P 1 x U5P
Ligand GOL 2 x GOL
1 modified residue:
Ligand CME 1 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 78.12Å b: 116.7Å c: 61.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.134 0.133 0.152
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Specificity in transition state binding: the Pauling model revisited.
Amyes et al. (2013)
9 other articles

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)