Research workbench
Secreted aspartic protease in complex with ritonavir
Analyse Secreted aspartic protease in complex with ritonavir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q70
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Candidapepsin-2
- EC
- 3.4.23.24
- UniProt
- P28871
- Ligands
- RIT, ZN
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Candidapepsin-2 (EC 3.4.23.24) | protein | 334 | 10% helix, 49% strand | P28871 |
Ligands and binding sites
- RIT · Ritonavir · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- MRD · (4R)-2-methylpentane-2,4-diol · additive · 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 | 260 | 0.53 | 0.76 | 33 | RIT |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3Q70 · Secreted aspartic protease in complex with ritonavir · 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 P28871
- Elsewhere: RCSB PDB 3Q70 · PDBe 3Q70 · UniProt P28871
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