PDBe 1brc

X-ray diffraction
2.5Å resolution

RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET OF TRYPSIN

Released:
Source organisms:
Primary publication:
Relocating a negative charge in the binding pocket of trypsin.
J. Mol. Biol. 230 934-49 (1993)
PMID: 8478942

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Anionic trypsin-2 Chain: E
Molecule details ›
Chain: E
Length: 223 amino acids
Theoretical weight: 23.81 KDa
Source organism: Rattus norvegicus
Expression system: unidentified
UniProt:
  • Canonical: P00763 (Residues: 24-246; Coverage: 97%)
Gene names: Prss2, Try2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Soluble APP-beta Chain: I
Molecule details ›
Chain: I
Length: 56 amino acids
Theoretical weight: 6.26 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 287-342; Coverage: 7%)
Gene names: A4, AD1, APP
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Factor Xa Inhibitor

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 93.1Å b: 93.1Å c: 62.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.168 not available
Expression systems:
  • unidentified
  • Not provided