MolNFT v1 · #11943 · protein
Combining mutations in HIV-1 protease to understand mechanisms of resistance
1K1U · Protease retropepsin: “Combining mutations in HIV-1 protease to understand mechanisms of resistance”. X-ray diffraction, 1 ligand (0Q4), 1 pocket (best druggability 0.71). MolNFT v1 #11943 on GenesisL1: 3D structure, binding sites…
- PDB
- 1K1U
- Type
- protein
- Length
- 198 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease retropepsin
- EC
- 3.4.23.16
- UniProt
- P04587
- Ligands
- 0Q4
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protease retropepsin (EC 3.4.23.16) | protein | 99 | 4% helix, 56% strand | P04587 |
Ligands and binding sites
- 0Q4 · N-[(2R)-2-({N~5~-[amino(iminio)methyl]-L-ornithyl-L-valyl}amino)-4-methylpentyl]-L-phenylalanyl-L-alpha-glutamyl-L-alanyl-L-norleucinamide · 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 | 345 | 0.71 | 0.83 | 38 | 0Q4 |
Interfaces
1 interface between chains.
- A–B · 1864 Ų buried · 40 hydrogen bonds · protein-protein
Compared structures
- 1K1U · Combining Mutations in HIV-1 Protease to Understand Mechanisms of Resistance · 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 P04587
- Elsewhere: RCSB PDB 1K1U · PDBe 1K1U · UniProt P04587
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