› 7dpw

Electron Microscopy
2.65Å resolution

Structural basis for ligand binding modes of CTP synthase

Released:
DOI: 10.2210/pdb7dpw/pdb
PDB entry 7dpw coloured by chain, front view.
PDB entry 7dpw coloured by chain, side view.
PDB entry 7dpw coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Structural basis for ligand binding modes of CTP synthase.
Zhou X, Guo CJ, Chang CC, Zhong J, Hu HH, Lu GM, Liu JL
OpenAccess logo Proc Natl Acad Sci U S A 118 (2021)
PMID: 34301892
Related structures: EMD-30811

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194307 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CTP synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 556 amino acids
Theoretical weight: 62.44 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: Q9VUL1 (Residues: 1-556; Coverage: 89%)
Gene names: CG45070, CTPsyn, Ctps
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand CTP 8 x CTP
Ligand MG 8 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.65Å
Relevant EMDB volumes: EMD-30811
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

2 review citations

GTP-Dependent Regulation of CTP Synthase: Evolving Insights into Allosteric Activation and NH3 Translocation.
Bearne et al. (2022)
1 more

1 mention without citation

Tunnel Architectures in Enzyme Systems that Transport Gaseous Substrates.
Singh et al. (2021)