› 1op2

X-ray diffraction
2.1Å resolution

Crystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutus

Released:
DOI: 10.2210/pdb1op2/pdb
PDB entry 1op2 coloured by chain, front view.
PDB entry 1op2 coloured by chain, side view.
PDB entry 1op2 coloured by chain, top view.
Source organism: Deinagkistrodon acutus
Primary publication:
Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases.
Zhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L
J Biol Chem 280 10524-9 (2005)
PMID: 15632114

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191513 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Snake venom serine protease Dav-PA Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 25.36 KDa
Source organism: Deinagkistrodon acutus
UniProt:
  • Canonical: Q9I8X1 (Residues: 25-258; Coverage: 98%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand NAG 1 x NAG
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 119.43Å b: 42.83Å c: 44.94Å
α: 90° β: 99.61° γ: 90°
R-values:
R R work R free
0.169 0.165 0.211

Quick links

Citations

1 review citation

Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis.
Kang et al. (2011)
25 other articles

1 mention without citation

The expanding diversity of serine hydrolases.
Botos et al. (2007)