1mtn

X-ray diffraction
2.8Å resolution

BOVINE ALPHA-CHYMOTRYPSIN:BPTI CRYSTALLIZATION

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero octamer
PDBe Complex ID:
PDB-CPX-133406 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Chymotrypsin A chain A Chains: A, E
Molecule details ›
Chains: A, E
Length: 13 amino acids
Theoretical weight: 1.25 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 1-13; Coverage: 5%)
Chymotrypsin A chain B Chains: B, F
Molecule details ›
Chains: B, F
Length: 131 amino acids
Theoretical weight: 13.93 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 16-146; Coverage: 54%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Chymotrypsin A chain C Chains: C, G
Molecule details ›
Chains: C, G
Length: 97 amino acids
Theoretical weight: 10.07 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 149-245; Coverage: 40%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Pancreatic trypsin inhibitor Chains: D, H
Molecule details ›
Chains: D, H
Length: 58 amino acids
Theoretical weight: 6.53 KDa
Source organism: Bos taurus
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: RIGAKU RUH2R
Spacegroup: P61
Unit cell:
a: 102.45Å b: 102.45Å c: 207.57Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
not available not available 0.24