Research workbench
Acetyl-CYPA:HIV-1 N-term capsid domain complex
Analyse Acetyl-CYPA:HIV-1 N-term capsid domain complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X2D
- Type
- protein
- Length
- 611 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P62937, P12493
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 165 | — | P62937 |
| C | — | protein | 164 | — | P62937 |
| D | — | protein | 146 | — | P12493 |
| E | — | protein | 136 | — | P12493 |
Compared structures
- 2X2D · acetyl-CypA:HIV-1 N-term capsid domain complex · the same entry in another collection · chain B against B, 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 P62937
- Every structure of UniProt P12493
- Elsewhere: RCSB PDB 2X2D · PDBe 2X2D · UniProt P62937 · UniProt P12493
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