Research workbench
Aspergillopepsin from aspergillus phoenicis
Analyse Aspergillopepsin from aspergillus phoenicis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IBQ
- Type
- protein
- Length
- 650 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspergillopepsin
- EC
- 3.4.23.18
- UniProt
- Q12567
- Ligands
- MAN, ZN
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspergillopepsin (EC 3.4.23.18) | protein | 325 | 12% helix, 45% strand | Q12567 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B
- ZN · Zinc ion · metal · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 466 | 0.62 | 0.76 | 45 | ZN |
| 2 | 330 | 0.54 | 0.74 | 34 | empty |
| 3 | 61 | 0.27 | 0.73 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 498 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 glycan, 2 disulfide (O-glycosylation, disulfide).
Compared structures
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 Q12567
- Elsewhere: RCSB PDB 1IBQ · PDBe 1IBQ · UniProt Q12567
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