› 1c3u

X-ray diffraction
2.3Å resolution

T. MARITIMA ADENYLOSUCCINATE LYASE

Released:
DOI: 10.2210/pdb1c3u/pdb
PDB entry 1c3u coloured by chain, front view.
PDB entry 1c3u coloured by chain, side view.
PDB entry 1c3u coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway.
Toth EA, Yeates TO
Structure 8 163-74 (2000)
PMID: 10673438

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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194718 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylosuccinate lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 431 amino acids
Theoretical weight: 49.95 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0I0 (Residues: 1-431; Coverage: 100%)
Gene names: TM_1095, purB
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: C2221
Unit cell:
a: 120.498Å b: 126.213Å c: 169.048Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.23
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

3 mentions without citation

Connectivity independent protein-structure alignment: a hierarchical approach.
Kolbeck et al. (2006)
2 more