Research workbench
Structure of the protease from simian immunodeficiency virus: complex with an irreversible non-peptide inhibitor
Analyse Structure of the protease from simian immunodeficiency virus: complex with an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2SAM
- Type
- protein
- Length
- 99 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SIV protease
- UniProt
- Q88016
- Ligands
- EPN
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SIV protease | protein | 99 | 6% helix, 48% strand | Q88016 |
Ligands and binding sites
- EPN · 3-(4-nitro-phenoxy)-propan-1-ol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.42 | 0.77 | 16 | empty |
| 2 | 80 | 0.33 | 0.74 | 19 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2SAM · Structure of the protease from simian immunodeficiency virus: complex with an… · 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 Q88016
- Elsewhere: RCSB PDB 2SAM · PDBe 2SAM · UniProt Q88016
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