MolNFT v1 · #121440 · protein
Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0-ångströms resolution
5HVP · HIV-1 protease: “Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and…”. X-ray diffraction, 2 ligands (ACE, CL). MolNFT v1 #121440 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5HVP
- Type
- protein
- Length
- 203 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV-1 protease; Acetyl-*pepstatin
- UniProt
- Q9WFL7
- Ligands
- ACE, CL
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | HIV-1 protease | protein | 99 | 7% helix, 58% strand | Q9WFL7 |
| C | Acetyl-*pepstatin | protein | 5 | 0% helix, 40% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 1857 Ų buried · 37 hydrogen bonds · protein-protein
- B–C · 462 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 431 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified, 1 covalent (nonstandard, covalent ligand).
Compared structures
- 5HVP · Crystallographic analysis of a complex between human immunodeficiency virus type 1… · 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 Q9WFL7
- Elsewhere: RCSB PDB 5HVP · PDBe 5HVP · UniProt Q9WFL7
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