› 1iac

X-ray diffraction
2.1Å resolution

REFINED 1.8 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF ASTACIN, A ZINC-ENDOPEPTIDASE FROM THE CRAYFISH ASTACUS ASTACUS L. STRUCTURE DETERMINATION, REFINEMENT, MOLECULAR STRUCTURE AND COMPARISON WITH THERMOLYSIN

Released:
DOI: 10.2210/pdb1iac/pdb
PDB entry 1iac coloured by chain, front view.
PDB entry 1iac coloured by chain, side view.
PDB entry 1iac coloured by chain, top view.
Source organism: Astacus astacus
Primary publication:
Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin.
Gomis-Rüth FX, Stöcker W, Huber R, Zwilling R, Bode W
J Mol Biol 229 945-68 (1993)
PMID: 8445658

Function and Biology Details

Reaction catalysed: 
Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139644 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Astacin Chain: A
Molecule details ›
Chain: A
Length: 200 amino acids
Theoretical weight: 22.62 KDa
Source organism: Astacus astacus
Expression system: Not provided
UniProt:
  • Canonical: P07584 (Residues: 50-249; Coverage: 85%)
Sequence domains: Astacin (Peptidase family M12A)
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

1 bound ligand:
Ligand HG 1 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 61.92Å b: 61.92Å c: 98.57Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.16 0.16 not available
Expression system: Not provided

Quick links

Citations

8 review citations

Families of zinc metalloproteases.
Hooper NM. (1994)
7 more

2 mentions without citation

Architecture and function of metallopeptidase catalytic domains.
Cerdà-Costa et al. (2014)
1 more