Research workbench
Structure at 2.5-ångströms resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene*-based inhibitor
Analyse Structure at 2.5-ångströms resolution of chemically synthesized human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8HVP
- Type
- protein
- Length
- 205 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV-1 protease; Inhibitor val-ser-gln-asn-leu-PSI(CH(OH)-CH2)-val-ile-val (U-85548E)
- UniProt
- P03369
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | HIV-1 protease | protein | 99 | 4% helix, 45% strand | P03369 |
| I | Inhibitor val-ser-gln-asn-leu-PSI(CH(OH)-CH2)-val-ile-val (U-85548E) | protein | 7 | 0% helix, 43% strand | — |
Interfaces
3 interfaces between chains.
- A–B · 1853 Ų buried · 31 hydrogen bonds · protein-protein
- A–I · 533 Ų buried · 10 hydrogen bonds · protein-protein
- B–I · 473 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (nonstandard).
Compared structures
- 8HVP · Structure at 2.5-ångströms resolution of chemically synthesized human immunodeficiency… · 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 P03369
- Elsewhere: RCSB PDB 8HVP · PDBe 8HVP · UniProt P03369
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