Research workbench
Crystal structure of fiv capsid C-terminal domain
Analyse Crystal structure of fiv capsid C-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DCK
- Type
- protein
- Length
- 143 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid C-terminal domain
- UniProt
- P16087
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid C-terminal domain | protein | 71 | 59% helix, 0% strand | P16087 |
| B | Capsid C-terminal domain | protein | 72 | 58% helix, 0% strand | P16087 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.50 | 0.82 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 655 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5DCK · Crystal Structure of FIV Capsid C-Terminal Domain · 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 P16087
- Elsewhere: RCSB PDB 5DCK · PDBe 5DCK · UniProt P16087
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