› 1p2q

X-ray diffraction
1.8Å resolution

Structural consequences of accommodation of four non-cognate amino-acid residues in the S1 pocket of bovine trypsin and chymotrypsin

Released:
DOI: 10.2210/pdb1p2q/pdb
PDB entry 1p2q coloured by chain, front view.
PDB entry 1p2q coloured by chain, side view.
PDB entry 1p2q coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structural consequences of accommodation of four non-cognate amino acid residues in the S1 pocket of bovine trypsin and chymotrypsin.
Helland R, Czapinska H, Leiros I, Olufsen M, Otlewski J, Smalås AO
J Mol Biol 333 845-61 (2003)
PMID: 14568540

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

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-133428 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymotrypsinogen A Chains: A, C
Molecule details ›
Chains: A, C
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
Pancreatic trypsin inhibitor Chains: B, D
Molecule details ›
Chains: B, D
Length: 58 amino acids
Theoretical weight: 6.53 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
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

2 bound ligands:
Ligand SO4 10 x SO4
Ligand TRS 2 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P61
Unit cell:
a: 99.57Å b: 99.57Å c: 205.22Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The many faces of protease-protein inhibitor interaction.
Otlewski et al. (2005)
10 other articles

1 mention without citation

Fluorine-induced polarity increases inhibitory activity of BPTI towards chymotrypsin.
Leppkes et al. (2022)