MolNFT v1 · #47006 · protein
Arfgap domain of HIV-1 rev binding protein
2OLM · Nucleoporin-like protein rip: “Arfgap domain of HIV-1 rev binding protein”. X-ray diffraction, 4 ligands (UNL, ZN, UNX), 1 pocket (best druggability 0.44). MolNFT v1 #47006 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2OLM
- Type
- protein
- Length
- 133 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoporin-like protein rip
- UniProt
- P52594
- Ligands
- UNL, ZN, UNX, SO4
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoporin-like protein rip | protein | 133 | 49% helix, 7% strand | P52594 |
Ligands and binding sites
- UNL · Unknown ligand · ligand · chains A
- ZN · Zinc ion · metal · chains A
- UNX · Unknown atom or ion · ion · 9 copies · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · chains A
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 | 120 | 0.44 | 0.77 | 21 | empty |
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 P52594
- Elsewhere: RCSB PDB 2OLM · PDBe 2OLM · UniProt P52594
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