1uhb

X-ray diffraction
2.15Å resolution

Crystal structure of porcine alpha trypsin bound with auto catalyticaly produced native peptide at 2.15 A resolution

Released:
Source organism: Sus scrofa
Primary publication:
Trypsin activity reduced by an autocatalytically produced nonapeptide.
J Biomol Struct Dyn 21 737-44 (2004)
PMID: 15106996

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133377 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Trypsin Chain: A
Molecule details ›
Chain: A
Length: 125 amino acids
Theoretical weight: 13.3 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P00761 (Residues: 9-133; Coverage: 54%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Trypsin Chain: B
Molecule details ›
Chain: B
Length: 98 amino acids
Theoretical weight: 10.21 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P00761 (Residues: 134-231; Coverage: 42%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Trypsin Chain: P
Molecule details ›
Chain: P
Length: 9 amino acids
Theoretical weight: 897 Da
Source organism: Sus scrofa
UniProt:
  • Canonical: P00761 (Residues: 177-185; Coverage: 4%)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 46.945Å b: 53.921Å c: 77.245Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.228