Research workbench
The crystal structures at 2.2 ångströms resolution of hydroxyethylene- based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations
Analyse The crystal structures at 2.2 ångströms resolution of hydroxyethylene- based… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HEF
- Type
- protein
- Length
- 104 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P03366
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | — | protein | 99 | — | P03366 |
| I | — | protein | 5 | — | — |
Compared structures
- 1HEF · The crystal structures at 2.2 angstroms resolution of hydroxyethylene-based inhibitors… · the same entry in another collection · chain E against E, 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 P03366
- Elsewhere: RCSB PDB 1HEF · PDBe 1HEF · UniProt P03366
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