X-ray diffraction
1.93Å resolution

Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities.


Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Snake venom metalloproteinase BaP1 Chain: A
Molecule details ›
Chain: A
Length: 202 amino acids
Theoretical weight: 22.75 KDa
Source organism: Bothrops asper
  • Canonical: P83512 (Residues: 193-394; Coverage: 52%)
Sequence domains: Reprolysin (M12B) family zinc metalloprotease
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P212121
Unit cell:
a: 38.425Å b: 60.364Å c: 86.257Å
α: 90° β: 90° γ: 90°
R R work R free
0.191 0.191 0.216