› 1dpj

X-ray diffraction
1.8Å resolution

THE STRUCTURE OF PROTEINASE A COMPLEXED WITH IA3 PEPTIDE INHIBITOR

Released:
DOI: 10.2210/pdb1dpj/pdb
PDB entry 1dpj coloured by chain, front view.
PDB entry 1dpj coloured by chain, side view.
PDB entry 1dpj coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.
Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A
Nat Struct Biol 7 113-7 (2000)
PMID: 10655612

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-133938 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Saccharopepsin Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 35.77 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P07267 (Residues: 77-405; Coverage: 86%)
Gene names: P2585, PEP4, PHO9, PRA1, YPL154C
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Protease A inhibitor 3 Chain: B
Molecule details ›
Chain: B
Length: 33 amino acids
Theoretical weight: 3.69 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P01094 (Residues: 2-34; Coverage: 49%)
Gene names: PAI3, YM8010.04C, YMR174C
Sequence domains: Saccharopepsin inhibitor I34

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
2 bound ligands:
Ligand NAG 1 x NAG
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P6222
Unit cell:
a: 191.66Å b: 191.66Å c: 52.08Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.192 0.213
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling.
Uversky et al. (2005)
11 more

6 mentions without citation

Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
Andreeva et al. (2001)
5 more