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Structural implications of drug resistant mutants of HIV-1 protease: high resolution crystal structures of the mutant PROTEASE/SUBSTRATE analog complexes.
Analyse Structural implications of drug resistant mutants of HIV-1 protease: high… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FF0
- Type
- protein
- Length
- 199 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04587
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 100 | — | P04587 |
| D | — | protein | 99 | — | P04587 |
Compared structures
- 1FF0 · Structural implications of drug resistant mutants of HIV-1 protease: high resolution… · the same entry in another collection · chain C against C, 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 1FF0 · PDBe 1FF0 · UniProt P04587
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