MolNFT v1 · #4862 · protein
Small G protein ARF6-GDP
1E0S · ADP-ribosylation factor 6: “Small G protein ARF6-GDP”. X-ray diffraction, 2 ligands (GDP, NH4), 1 pocket (best druggability 0.33). MolNFT v1 #4862 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1E0S
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor 6
- UniProt
- P62330
- Ligands
- GDP, NH4
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosylation factor 6 | protein | 173 | 36% helix, 29% strand | P62330 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- NH4 · Ammonium ion · ion · chains A
- BME · Beta-mercaptoethanol · 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 | 68 | 0.33 | 0.76 | 21 | NH4 |
Modifications
Observed in the structure: 1 covalent (additive adduct).
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 P62330
- Elsewhere: RCSB PDB 1E0S · PDBe 1E0S · UniProt P62330
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