PDBe 1flh

X-ray diffraction
2.45Å resolution

CRYSTAL STRUCTURE OF HUMAN UROPEPSIN AT 2.45 A RESOLUTION

Released:
Source organism: Homo sapiens
Primary publication:
Structure of human uropepsin at 2.45 A resolution.
Acta Crystallogr. D Biol. Crystallogr. 57 1560-70 (2001)
PMID: 11679720

Function and Biology Details

Reaction catalysed:
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pepsin A-4 Chain: A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 34.62 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P0DJD7 (Residues: 63-388; Coverage: 87%)
Gene name: PGA4
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P212121
Unit cell:
a: 50.989Å b: 75.557Å c: 89.896Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.161 not available