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Crystal structure of the HIV-1 capsid protein C-terminal domain (146- 231) in complex with a camelid vhh.
Analyse Crystal structure of the HIV-1 capsid protein C-terminal domain (146- 231) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XT1
- Type
- protein
- Length
- 200 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gag polyprotein; Camelid vhh 9
- UniProt
- Q71B32
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gag polyprotein | protein | 86 | 53% helix, 1% strand | Q71B32 |
| B | Camelid vhh 9 | protein | 114 | 5% helix, 52% strand | — |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 827 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2XT1 · Crystal structure of the HIV-1 capsid protein C-terminal domain (146- 231) in 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 Q71B32
- Elsewhere: RCSB PDB 2XT1 · PDBe 2XT1 · UniProt Q71B32
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