› 2wea

X-ray diffraction
1.25Å resolution

ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.20) COMPLEX WITH PHOSPHONATE INHIBITOR: METHYL[CYCLO-7[(2R)-((N-VALYL) AMINO)-2-(HYDROXYL-(1S)-1-METHYOXYCARBONYL-2-PHENYLETHOXY) PHOSPHINYLOXY-ETHYL]-1-NAPHTHALENEACETAMIDE], SODIUM SALT

Released:
DOI: 10.2210/pdb2wea/pdb
PDB entry 2wea coloured by chain, front view.
PDB entry 2wea coloured by chain, side view.
PDB entry 2wea coloured by chain, top view.
Source organism: Penicillium janthinellum
Primary publication:
Macrocyclic Inhibitors of Penicillopepsin. II. X-Ray Crystallographic Analyses of Penicillopepsin Complexed with a P3-P1 Macrocyclic Peptidyl Inhibitor and with its Two Acyclic Analogues
Ding J, Fraser ME, Meyer JH, Bartlett PA, James MNG
J. Am. Chem. Soc. 120 4610-4621 (1998)

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133576 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Penicillopepsin-1 Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 33.47 KDa
Source organism: Penicillium janthinellum
UniProt:
  • Canonical: P00798 (Residues: 1-323; Coverage: 100%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

3 bound ligands:
Ligand MAN 2 x MAN
Ligand SO4 1 x SO4
Ligand PP6 1 x PP6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: C2
Unit cell:
a: 96.33Å b: 46.27Å c: 64.59Å
α: 90° β: 115.1° γ: 90°
R-values:
R R work R free
0.149 0.145 0.19

Quick links

Citations

6 mentions without citation

Cation-pi interactions in structural biology.
Gallivan et al. (1999)
5 more