MolNFT v1 · #120951 · protein
HIV-1 ca N-terminal domain, open conformation
5HGK · Capsid protein: “HIV-1 ca N-terminal domain, open conformation”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.32). MolNFT v1 #120951 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5HGK
- Type
- protein
- Length
- 292 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein
- UniProt
- D2ECE2
- Ligands
- CL
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Capsid protein | protein | 146 | 58% helix, 4% strand | D2ECE2 |
Ligands and binding sites
- CL · Chloride ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 92 | 0.32 | 0.73 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 550 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5HGK · HIV-1 CA N-terminal domain, open conformation · 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 D2ECE2
- Elsewhere: RCSB PDB 5HGK · PDBe 5HGK · UniProt D2ECE2
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