› 2kai

X-ray diffraction
2.5Å resolution

REFINED 2.5 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BY PORCINE KALLIKREIN A AND THE BOVINE PANCREATIC TRYPSIN INHIBITOR. CRYSTALLIZATION, PATTERSON SEARCH, STRUCTURE DETERMINATION, REFINEMENT, STRUCTURE AND COMPARISON WITH ITS COMPONENTS AND WITH THE BOVINE TRYPSIN-PANCREATIC TRYPSIN INHIBITOR COMPLEX

Released:
DOI: 10.2210/pdb2kai/pdb
PDB entry 2kai coloured by chain, front view.
PDB entry 2kai coloured by chain, side view.
PDB entry 2kai coloured by chain, top view.
Source organisms:
Primary publication:
Refined 2.5 A X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. Crystallization, Patterson search, structure determination, refinement, structure and comparison with its components and with the bovine trypsin-pancreatic trypsin inhibitor complex.
Chen Z, Bode W
J Mol Biol 164 283-311 (1983)
PMID: 6188842

Function and Biology Details

Reaction catalysed: 
Preferential cleavage of Arg-|- bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|- or Leu-|-. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-|- bonds (5).
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133313 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Glandular kallikrein Chain: A
Molecule details ›
Chain: A
Length: 80 amino acids
Theoretical weight: 9.12 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P00752 (Residues: 8-87; Coverage: 33%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Glandular kallikrein Chain: B
Molecule details ›
Chain: B
Length: 152 amino acids
Theoretical weight: 16.51 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P00752 (Residues: 95-148, 150-170, 172-174, 176-246; Coverage: 61%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Pancreatic trypsin inhibitor Chain: I
Molecule details ›
Chain: I
Length: 58 amino acids
Theoretical weight: 6.53 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 106.2Å b: 106.2Å c: 108.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 not available
Expression system: Not provided

Quick links

Citations

12 review citations

Natural protein proteinase inhibitors and their interaction with proteinases.
Bode et al. (1992)
11 more

27 mentions without citation

Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs).
Goettig et al. (2010)
26 more