Research workbench
Crystal structure of actinohivin; potent anti-HIV protein
Analyse Crystal structure of actinohivin; potent anti-HIV protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A07
- Type
- protein
- Length
- 234 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actinohivin
- UniProt
- Q9KWN0
- Ligands
- NA
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actinohivin | protein | 116 | 8% helix, 40% strand | Q9KWN0 |
| B | Actinohivin | protein | 118 | 8% helix, 39% strand | Q9KWN0 |
Ligands and binding sites
- NA · Sodium ion · metal · 6 copies · chains A, 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.56 | 0.82 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 296 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 Q9KWN0
- Elsewhere: RCSB PDB 3A07 · PDBe 3A07 · UniProt Q9KWN0
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