› 2gcq

X-ray diffraction
2Å resolution

Fully ligated E.Coli Adenylosuccinate Synthetase with GTP, 2'-deoxy-IMP and Hadacidin

Released:
DOI: 10.2210/pdb2gcq/pdb
PDB entry 2gcq coloured by chain, front view.
PDB entry 2gcq coloured by chain, side view.
PDB entry 2gcq coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Cavitation as a mechanism of substrate discrimination by adenylosuccinate synthetases.
Iancu CV, Zhou Y, Borza T, Fromm HJ, Honzatko RB
Biochemistry 45 11703-11 (2006)
PMID: 16981730

Function and Biology Details

Reaction catalysed: 
GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-532081 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylosuccinate synthetase Chain: A
Molecule details ›
Chain: A
Length: 431 amino acids
Theoretical weight: 47.27 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7D4 (Residues: 2-432; Coverage: 100%)
Gene names: JW4135, adeK, b4177, purA
Sequence domains: Adenylosuccinate synthetase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand MG 1 x MG
Ligand DOI 1 x DOI
Ligand GDP 1 x GDP
Ligand HDA 1 x HDA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 80.585Å b: 80.585Å c: 158.46Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.265 0.224 0.25
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Mechanisms supporting aminoadenine-based viral DNA genomes.
Kaminski PA. (2021)
3 other articles

3 mentions without citation

Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA.
Czernecki et al. (2021)
2 more