PDBe 1am5

X-ray diffraction
2.16Å resolution

THE CRYSTAL STRUCTURE AND PROPOSED AMINO ACID SEQUENCE OF A PEPSIN FROM ATLANTIC COD (GADUS MORHUA)

Released:
Source organism: Gadus morhua
Primary publication:
Structure and proposed amino-acid sequence of a pepsin from atlantic cod (Gadus morhua).
Acta Crystallogr. D Biol. Crystallogr. 54 32-46 (1998)
PMID: 9761815

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-2B Chain: A
Molecule details ›
Chain: A
Length: 324 amino acids
Theoretical weight: 34.03 KDa
Source organism: Gadus morhua
UniProt:
  • Canonical: P56272 (Residues: 1-324; Coverage: 100%)
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: BRUKER NONIUS
Spacegroup: P212121
Unit cell:
a: 35.98Å b: 75.4Å c: 108.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.224