› 1c3c

X-ray diffraction
1.8Å resolution

T. MARITIMA ADENYLOSUCCINATE LYASE

Released:
DOI: 10.2210/pdb1c3c/pdb
PDB entry 1c3c coloured by chain, front view.
PDB entry 1c3c coloured by chain, side view.
PDB entry 1c3c 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: 429 amino acids
Theoretical weight: 49.69 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0I0 (Residues: 2-430; Coverage: 100%)
Gene names: TM_1095, purB
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: C2221
Unit cell:
a: 120.809Å b: 126.753Å c: 169Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.207
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

4 mentions without citation

The natural history of biocatalytic mechanisms.
Nath et al. (2014)
3 more