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Structure of human ADP-ribosylation factor-like 5 (ARL5)

Analyse Structure of human ADP-ribosylation factor-like 5 (ARL5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2H17
Type: protein
Length: 160 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribosylation factor-like protein 5A
UniProt: Q9Y689
Ligands: GDP, UNX
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ADP-ribosylation factor-like protein 5A	protein	160	33% helix, 29% strand	Q9Y689

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
UNX · Unknown atom or ion · ion · 3 copies · 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	115	0.45	0.77	16	empty

Compared structures

2H17 · Structure of human ADP-ribosylation factor-like 5 (ARL5) · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y689 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor-like protein 5A (Q9Y689) · a predicted model of the same protein · chain A against A, TM-score 0.87

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 Q9Y689
Elsewhere: RCSB PDB 2H17 · PDBe 2H17 · UniProt Q9Y689

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