› 7mig

Electron Microscopy
2.9Å resolution

Human CTPS1 bound to inhibitor T35

Released:
DOI: 10.2210/pdb7mig/pdb
PDB entry 7mig coloured by chain, front view.
PDB entry 7mig coloured by chain, side view.
PDB entry 7mig coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for isoform-specific inhibition of human CTPS1.
Lynch EM, DiMattia MA, Albanese S, van Zundert GCP, Hansen JM, Quispe JD, Kennedy MA, Verras A, Borrelli K, Toms AV, Kaila N, Kreutter KD, McElwee JJ, Kollman JM
Proc Natl Acad Sci U S A 118 (2021)
PMID: 34583994
Related structures: EMD-23850

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 analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148184 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CTP synthase 1 Chains: A, B, C, E
Molecule details ›
Chains: A, B, C, E
Length: 591 amino acids
Theoretical weight: 66.78 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
  • Canonical: P17812 (Residues: 1-591; Coverage: 100%)
Gene names: CTPS, CTPS1
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand ZFY 4 x ZFY
Ligand GLN 4 x GLN
Ligand MG 4 x MG
Ligand UTP 4 x UTP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.9Å
Relevant EMDB volumes: EMD-23850
Expression system: unidentified baculovirus

Quick links

Citations

3 review citations

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