› 1gl0

X-ray diffraction
3Å resolution

structure of the complex between bovine alpha-chymotrypsin and PMP-D2v, an inhibitor from the insect Locusta migratoria

Released:
DOI: 10.2210/pdb1gl0/pdb
PDB entry 1gl0 coloured by chain, front view.
PDB entry 1gl0 coloured by chain, side view.
PDB entry 1gl0 coloured by chain, top view.
Source organisms:
Primary publication:
Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity.
Roussel A, Mathieu M, Dobbs A, Luu B, Cambillau C, Kellenberger C
J Biol Chem 276 38893-8 (2001)
PMID: 11495915

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133433 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymotrypsinogen A Chain: E
Molecule details ›
Chain: E
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 1-245; Coverage: 100%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Protease inhibitor LCMI-I Chain: I
Molecule details ›
Chain: I
Length: 35 amino acids
Theoretical weight: 3.72 KDa
Source organism: Locusta migratoria
Expression system: Not provided
UniProt:
  • Canonical: P80060 (Residues: 20-54; Coverage: 48%)
Sequence domains: Pacifastin inhibitor (LCMII)

Ligands and Environments

1 bound ligand:
Ligand CD 3 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P6522
Unit cell:
a: 85.853Å b: 85.853Å c: 187.983Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.174 0.198
Expression system: Not provided

Quick links

Citations

3 review citations

Mechanisms of macromolecular protease inhibitors.
Farady et al. (2010)
2 more

5 mentions without citation

Monospecific inhibitors show that both mannan-binding lectin-associated serine protease-1 (MASP-1) and -2 Are essential for lectin pathway activation and reveal structural plasticity of MASP-2.
Héja et al. (2012)
4 more