› 7d95

X-ray diffraction
1.67Å resolution

Crystal structure of acivicin-bound GATase subunit of Methanocaldococcus jannaschii GMP synthetase

Released:
DOI: 10.2210/pdb7d95/pdb
PDB entry 7d95 coloured by chain, front view.
PDB entry 7d95 coloured by chain, side view.
PDB entry 7d95 coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii DSM 2661
Primary publication:
Structural basis for the hyperthermostability of an archaeal enzyme induced by succinimide formation.
Dongre AV, Das S, Bellur A, Kumar S, Chandrashekarmath A, Karmakar T, Balaram P, Balasubramanian S, Balaram H
Biophys J 120 3732-3746 (2021)
PMID: 34302792

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(4)(+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176720 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP synthase [glutamine-hydrolyzing] subunit A Chains: A, B
Molecule details ›
Chains: A, B
Length: 188 amino acids
Theoretical weight: 21.18 KDa
Source organism: Methanocaldococcus jannaschii DSM 2661
Expression system: Escherichia coli
UniProt:
  • Canonical: Q58970 (Residues: 1-188; Coverage: 100%)
Gene names: MJ1575, guaAA
Sequence domains: Glutamine amidotransferase class-I

Ligands and Environments

No bound ligands
2 modified residues:
Ligand 5CS 2 x 5CS
Ligand SNN 2 x SNN

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P32
Unit cell:
a: 65.35Å b: 65.35Å c: 97.371Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.196 0.234
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Locking out water at 100°C.
Smith JC. (2021)

2 mentions without citation

GMP Synthetase: Allostery, Structure, and Function.
Ballut et al. (2023)
1 more