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Small G protein ARF6-GDP

Analyse Small G protein ARF6-GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.33	0.76	21	NH4

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

1E0S · small G protein Arf6-GDP · the same entry in another collection · chain A against A, TM-score 1.00
P62330 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor 6 (P62330) · a predicted model of the same protein · chain A against A, TM-score 0.82

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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