› 1mc2

X-ray diffraction
0.85Å resolution

monomeric LYS-49 phospholipase A2 homologue purified from AG

Released:
DOI: 10.2210/pdb1mc2/pdb
PDB entry 1mc2 coloured by chain, front view.
PDB entry 1mc2 coloured by chain, side view.
PDB entry 1mc2 coloured by chain, top view.
Source organism: Deinagkistrodon acutus
Primary publication:
The crystal structure of a novel, inactive, lysine 49 PLA2 from Agkistrodon acutus venom: an ultrahigh resolution, AB initio structure determination.
Liu Q, Huang Q, Teng M, Weeks CM, Jelsch C, Zhang R, Niu L
J Biol Chem 278 41400-8 (2003)
PMID: 12871974

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-129587 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Basic phospholipase A2 homolog acutohaemolysin Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 14.09 KDa
Source organism: Deinagkistrodon acutus
UniProt:
  • Canonical: O57385 (Residues: 17-138; Coverage: 100%)
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

1 bound ligand:
Ligand IPA 2 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: C2
Unit cell:
a: 44.732Å b: 59.086Å c: 45.308Å
α: 90° β: 117.43° γ: 90°
R-values:
R R work R free
0.104 not available 0.121

Quick links

Citations

3 review citations

An overview of lysine-49 phospholipase A2 myotoxins from crotalid snake venoms and their structural determinants of myotoxic action.
Lomonte et al. (2003)
2 more

12 mentions without citation

The Extent of Cooperativity of Protein Motions Observed with Elastic Network Models Is Similar for Atomic and Coarser-Grained Models.
Sen et al. (2006)
11 more