1y43

X-ray diffraction
1.4Å resolution

crystal structure of aspergilloglutamic peptidase from Aspergillus niger

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage in B chain of insulin: 3-Asn-|-Gln-4, 13-Gly-|-Ala-14, and 26-Tyr-|-Thr-27.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-150268 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspergillopepsin-2 light chain Chain: A
Molecule details ›
Chain: A
Length: 39 amino acids
Theoretical weight: 3.92 KDa
Source organism: Aspergillus niger var. macrosporus
UniProt:
  • Canonical: P24665 (Residues: 60-98; Coverage: 15%)
Aspergillopepsin-2 heavy chain Chain: B
Molecule details ›
Chain: B
Length: 173 amino acids
Theoretical weight: 18.37 KDa
Source organism: Aspergillus niger var. macrosporus
UniProt:
  • Canonical: P24665 (Residues: 110-282; Coverage: 66%)
Sequence domains: Peptidase A4 family
Structure domains: Peptidase G1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 55.1Å b: 70.7Å c: 38.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.226