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Crystal structure of HIV1 protease in situ product complex
Analyse Crystal structure of HIV1 protease in situ product complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NPH
- Type
- protein
- Length
- 207 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease retropepsin; Tetrapeptide fragment; Pentapeptide fragment
- EC
- 3.4.23.16
- UniProt
- Q72874
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protease retropepsin (EC 3.4.23.16) | protein | 99 | 7% helix, 55% strand | Q72874 |
| S | Tetrapeptide fragment | protein | 4 | 0% helix, 50% strand | — |
| T | Pentapeptide fragment | protein | 5 | 0% helix, 40% strand | — |
Interfaces
6 interfaces between chains.
- A–B · 1893 Ų buried · 45 hydrogen bonds · protein-protein
- B–T · 361 Ų buried · 8 hydrogen bonds · protein-protein
- A–S · 344 Ų buried · 10 hydrogen bonds · protein-protein
- B–S · 236 Ų buried · 4 hydrogen bonds · protein-protein
- A–T · 215 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2NPH · Crystal structure of HIV1 protease in situ product complex · 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 Q72874
- Elsewhere: RCSB PDB 2NPH · PDBe 2NPH · UniProt Q72874
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