› 2pts

X-ray diffraction
2Å resolution

Crystal structure of wild type Escherichia coli adenylosuccinate lyase

Released:
DOI: 10.2210/pdb2pts/pdb
PDB entry 2pts coloured by chain, front view.
PDB entry 2pts coloured by chain, side view.
PDB entry 2pts coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism.
Tsai M, Koo J, Yip P, Colman RF, Segall ML, Howell PL
J Mol Biol 370 541-54 (2007)
PMID: 17531264

Function and Biology Details

Reaction catalysed: 
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylosuccinate lyase Chain: A
Molecule details ›
Chain: A
Length: 462 amino acids
Theoretical weight: 52.86 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AB89 (Residues: 1-456; Coverage: 100%)
Gene names: JW1117, b1131, purB
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 9 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: I222
Unit cell:
a: 68.374Å b: 98.406Å c: 136.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.165 0.202
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Structural biology of the purine biosynthetic pathway.
Zhang et al. (2008)
3 more

7 mentions without citation

State of the science of health literacy measures: Validity implications for minority populations.
Nguyen et al. (2015)
6 more