› 1gpm

X-ray diffraction
2.2Å resolution

ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE

Released:
DOI: 10.2210/pdb1gpm/pdb
PDB entry 1gpm coloured by chain, front view.
PDB entry 1gpm coloured by chain, side view.
PDB entry 1gpm coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL
Nat Struct Biol 3 74-86 (1996)
PMID: 8548458

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(4)(+)
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-137392 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP synthase [glutamine-hydrolyzing] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 525 amino acids
Theoretical weight: 58.75 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P04079 (Residues: 1-525; Coverage: 100%)
Gene names: JW2491, b2507, guaA
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand PO4 4 x PO4
Ligand POP 4 x POP
Ligand AMP 4 x AMP
Ligand CIT 4 x CIT
Ligand MG 3 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 156Å b: 102Å c: 78.8Å
α: 90° β: 96.7° γ: 90°
R-values:
R R work R free
0.174 0.174 not available
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Channeling of substrates and intermediates in enzyme-catalyzed reactions.
Huang et al. (2001)
17 more

19 mentions without citation

Adenylating enzymes in Mycobacterium tuberculosis as drug targets.
Duckworth et al. (2012)
18 more