› 1vcm

X-ray diffraction
2.35Å resolution

Crystal Structure of T.th. HB8 CTP synthetase

Released:
DOI: 10.2210/pdb1vcm/pdb
PDB entry 1vcm coloured by chain, front view.
PDB entry 1vcm coloured by chain, side view.
PDB entry 1vcm coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine binding sites.
Goto M, Omi R, Nakagawa N, Miyahara I, Hirotsu K
Structure 12 1413-23 (2004)
PMID: 15296735

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177947 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CTP synthase Chain: A
Molecule details ›
Chain: A
Length: 550 amino acids
Theoretical weight: 61.09 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SIA8 (Residues: 1-550; Coverage: 100%)
Gene names: TTHA1466, pyrG
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I222
Unit cell:
a: 86Å b: 120.67Å c: 143.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.235 0.279
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Gates of enzymes.
Gora et al. (2013)
7 more

4 mentions without citation

Crystal structure of Escherichia coli cytidine triphosphate synthetase, a nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase fusion protein and homologue of anticancer and antiparasitic drug targets.
Endrizzi et al. (2004)
3 more