Research workbench
Secreted aspartic proteinase (sap) 3 from candida albicans
Analyse Secreted aspartic proteinase (sap) 3 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
- 2H6S
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Candidapepsin-3
- EC
- 3.4.23.24
- UniProt
- P43092
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Candidapepsin-3 (EC 3.4.23.24) | protein | 340 | 10% helix, 45% strand | P43092 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.53 | 0.74 | 39 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2H6S · Secreted aspartic proteinase (Sap) 3 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 P43092
- Elsewhere: RCSB PDB 2H6S · PDBe 2H6S · UniProt P43092
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