Research workbench
Viability of a drug-resistant HIV-1 protease mutant: structural insights for better antiviral therapy
Analyse Viability of a drug-resistant HIV-1 protease mutant: structural insights for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MTB
- Type
- protein
- Length
- 200 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease retropepsin
- EC
- 3.4.23.16
- UniProt
- P03369
- Ligands
- QNC, DIQ, NTB
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease retropepsin (EC 3.4.23.16) | protein | 101 | 7% helix, 55% strand | P03369 |
| B | Protease retropepsin (EC 3.4.23.16) | protein | 99 | 7% helix, 55% strand | P03369 |
Ligands and binding sites
- QNC · quinoline-2-carboxylic acid · ligand · chains A, B
- DIQ · 2-methyl-decahydro-isoquinoline-3-carboxylic acid · ligand · chains A, B
- NTB · Tertiary-butylamine · ligand · 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 | 221 | 0.64 | 0.82 | 27 | DIQ, NTB |
Interfaces
1 interface between chains.
- A–B · 1934 Ų buried · 39 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
- 1MTB · Viability of a drug-resistant HIV-1 protease mutant: structural insights for better… · the same entry in another collection · chain B against B, 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 P03369
- Elsewhere: RCSB PDB 1MTB · PDBe 1MTB · UniProt P03369
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