1tev

X-ray diffraction
2.1Å resolution

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

Released:
Source organism: Homo sapiens
Primary publication:
Substrate-induced conformational changes in human UMP/CMP kinase.
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
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (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:
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)