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Structure of human ADP-ribosylation factor-like 5

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

PDB
1Z6Y
Type
protein
Length
338 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ADP-ribosylation factor-like protein 5
UniProt
Q9Y689
Ligands
GDP
Pockets
3 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BADP-ribosylation factor-like protein 5protein16931% helix, 28% strandQ9Y689

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12000.460.7532empty
2940.420.7817empty
3690.370.7815empty

Interfaces

1 interface between chains.

  • A–B · 470 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 1Z6Y · Structure Of Human ADP-Ribosylation Factor-Like 5 · 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 B against A, TM-score 0.81

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