1iae

X-ray diffraction
1.83Å resolution

CRYSTAL STRUCTURES, SPECTROSCOPIC FEATURES, AND CATALYTIC PROPERTIES OF COBALT(II), COPPER(II), NICKEL(II), AND MERCURY(II) DERIVATIVES OF THE ZINC ENDOPEPTIDASE ASTACIN. A CORRELATION OF STRUCTURE AND PROTEOLYTIC ACTIVITY

Released:

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

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:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 61.89Å b: 61.89Å c: 98.55Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.143 0.143 not available
Expression system: Not provided