Research workbench
Secreted aspartic proteinase (sap) 1 from candida albicans
Analyse Secreted aspartic proteinase (sap) 1 from candida albicans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QZW
- Type
- protein
- Length
- 682 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Candidapepsin-1
- EC
- 3.4.23.24
- UniProt
- P28872
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Candidapepsin-1 (EC 3.4.23.24) | protein | 341 | 9% helix, 47% strand | P28872 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.64 | 0.80 | 47 | empty |
| 2 | 317 | 0.55 | 0.75 | 46 | empty |
| 3 | 165 | 0.42 | 0.73 | 24 | empty |
| 4 | 147 | 0.41 | 0.74 | 36 | empty |
| 5 | 52 | 0.26 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 687 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2QZW · Secreted aspartic proteinase (Sap) 1 from Candida albicans · 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 P28872
- Elsewhere: RCSB PDB 2QZW · PDBe 2QZW · UniProt P28872
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