2vkt

X-ray diffraction
2.5Å resolution

HUMAN CTP SYNTHETASE 2 - GLUTAMINASE DOMAIN

Released:
Source organism: Homo sapiens
Entry authors: Welin M, Tresaugues L, Arrowsmith CH, Berglund H, Busam RD, Collins R, Dahlgren LG, Edwards AM, Flodin S, Flores A, Graslund S, Hammarstrom M, Herman MD, Johansson I, Kallas A, Karlberg T, Kotenyova T, Lehtio L, Moche M, Nilsson ME, Nyman T, Persson C, Sagemark J, Svensson L, Thorsell AG, van den Berg S, Weigelt J, Nordlund P, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192555 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CTP synthase 2 Chain: A
Molecule details ›
Chain: A
Length: 289 amino acids
Theoretical weight: 32.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NRF8 (Residues: 292-562; Coverage: 46%)
Gene name: CTPS2
Sequence domains:
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: C2
Unit cell:
a: 105.2Å b: 73.1Å c: 50.5Å
α: 90° β: 95.6° γ: 90°
R-values:
R R work R free
0.209 0.207 0.239
Expression system: Escherichia coli BL21(DE3)