1p2o

X-ray diffraction
2Å resolution

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

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
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: 6.48 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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P61
Unit cell:
a: 100.17Å b: 100.17Å c: 206.14Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.227 0.227 0.253
Expression system: Escherichia coli BL21(DE3)