› 2cmy

X-ray diffraction
2.25Å resolution

Crystal complex between bovine trypsin and Veronica hederifolia trypsin inhibitor

Released:
DOI: 10.2210/pdb2cmy/pdb
PDB entry 2cmy coloured by chain, front view.
PDB entry 2cmy coloured by chain, side view.
PDB entry 2cmy coloured by chain, top view.
Source organisms:
Primary publication:
An unusual helix-turn-helix protease inhibitory motif in a novel trypsin inhibitor from seeds of Veronica (Veronica hederifolia L.).
Conners R, Konarev AV, Forsyth J, Lovegrove A, Marsh J, Joseph-Horne T, Shewry P, Brady RL
J Biol Chem 282 27760-8 (2007)
PMID: 17640870

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
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-133340 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease 1 Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Trypsin inhibitor Chain: B
Molecule details ›
Chain: B
Length: 34 amino acids
Theoretical weight: 4.06 KDa
Source organism: Veronica hederifolia
UniProt:
  • Canonical: P85981 (Residues: 1-34; Coverage: 100%)

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand CA 1 x CA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P212121
Unit cell:
a: 60.657Å b: 63.928Å c: 71.698Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.253

Quick links

Citations

9 review citations

Antimicrobial Peptides from Plants.
Tam et al. (2015)
8 more

1 mention without citation

Conformational changes of rBTI from buckwheat upon binding to trypsin: implications for the role of the P(8)' residue in the potato inhibitor I family.
Wang et al. (2011)