› 1tev

X-ray diffraction
2.1Å resolution

Crystal structure of the human UMP/CMP kinase in open conformation

Released:
DOI: 10.2210/pdb1tev/pdb
PDB entry 1tev coloured by chain, front view.
PDB entry 1tev coloured by chain, side view.
PDB entry 1tev coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Substrate-induced conformational changes in human UMP/CMP kinase.
Segura-Peña D, Sekulic N, Ort S, Konrad M, Lavie A
J Biol Chem 279 33882-9 (2004)
PMID: 15163660

Function and Biology Details

Reactions catalysed: 
ATP + (d)CMP = ADP + (d)CDP
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151632 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UMP-CMP kinase Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 22.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30085 (Residues: 1-196; Coverage: 100%)
Gene names: CMK, CMPK, CMPK1, UCK, UMK, UMPK
Sequence domains: Adenylate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P6522
Unit cell:
a: 62.75Å b: 62.75Å c: 226.31Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.222 0.216 0.275
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Prophylaxis and therapy of plague.
Oyston et al. (2013)
23 other articles

11 mentions without citation

Predicting the accuracy of protein-ligand docking on homology models.
Bordogna et al. (2011)
10 more