Research workbench
HIV-1 capsid C-terminal domain mutant (N183A)
Analyse HIV-1 capsid C-terminal domain mutant (N183A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DS5
- Type
- protein
- Length
- 292 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV-1 capsid protein
- UniProt
- Q72497
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | HIV-1 capsid protein | protein | 73 | 66% helix, 0% strand | Q72497 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.45 | 0.77 | 18 | empty |
| 2 | 53 | 0.44 | 0.83 | 16 | empty |
Interfaces
4 interfaces between chains.
- C–D · 803 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 793 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 505 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 42 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3DS5 · HIV-1 capsid C-terminal domain mutant (N183A) · 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 Q72497
- Elsewhere: RCSB PDB 3DS5 · PDBe 3DS5 · UniProt Q72497
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