Research workbench
Structure of the extracellular aspartic proteinase from candida tropicalis yeast.
Analyse Structure of the extracellular aspartic proteinase from candida tropicalis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1J71
- Type
- protein
- Length
- 338 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartic proteinase; Tetrapeptide thr-ile-thr-ser
- EC
- 3.4.23.24
- UniProt
- Q00663
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartic proteinase (EC 3.4.23.24) | protein | 334 | 10% helix, 49% strand | Q00663 |
| B | Tetrapeptide thr-ile-thr-ser | protein | 4 | 0% helix, 25% strand | — |
Ligands and binding sites
- EOH · Ethanol · additive · 6 copies · chains A, B
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 | 230 | 0.58 | 0.79 | 28 | EOH |
Interfaces
1 interface between chains.
- A–B · 339 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1J71 · Structure of the extracellular aspartic proteinase from Candida tropicalis yeast. · the same entry in another collection · chain A against A, TM-score 1.00
- Q00663 · AlphaFold monomer V2.0 prediction for candidapepsin (Q00663) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q00663
- Elsewhere: RCSB PDB 1J71 · PDBe 1J71 · UniProt Q00663
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