MolNFT v1 · #10703 · protein
Crystal structure of aspergillus oryzae aspartic proteinase complexed with pepstatin
1IZE: “Crystal structure of aspergillus oryzae aspartic proteinase complexed with pepstatin”. X-ray diffraction, 2 ligands (IVA, MAN), 1 pocket (best druggability 0.32). MolNFT v1 #10703 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1IZE
- Type
- protein
- Length
- 328 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartic proteinase; Pepstatin
- UniProt
- Q9URD0
- Ligands
- IVA, MAN
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartic proteinase | protein | 323 | 12% helix, 48% strand | Q9URD0 |
| B | Pepstatin | protein | 5 | 0% helix, 20% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.32 | 0.73 | 24 | IVA |
Interfaces
1 interface between chains.
- A–B · 570 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified, 1 covalent, 1 glycan (nonstandard, covalent ligand, O-glycosylation).
Compared structures
- 1IZE · Crystal structure of Aspergillus oryzae Aspartic proteinase complexed with pepstatin · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9URD0
- Elsewhere: RCSB PDB 1IZE · PDBe 1IZE · UniProt Q9URD0
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