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Comparison of the structures of HIV-2 protease complexes in three crystal space groups with an HIV-1 protease complex structure
Analyse Comparison of the structures of HIV-2 protease complexes in three crystal space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HPE
- Type
- protein
- Length
- 207 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04584
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 99 | — | P04584 |
| S | — | protein | 9 | — | — |
Compared structures
- 2HPE · Comparison of the structures of HIV-2 protease complexes in three crystal space groups… · 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 P04584
- Elsewhere: RCSB PDB 2HPE · PDBe 2HPE · UniProt P04584
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