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ARF1[DELTA 1-17]-GDP-mg in complex with brefeldin a and a SEC7 domain

Analyse ARF1[DELTA 1-17]-GDP-mg in complex with brefeldin a and a SEC7 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1S9D
Type
protein
Length
348 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ADP-ribosylation factor 1; Arno
UniProt
P84080, Q99418
Ligands
GDP, AFB, MG
Pockets
2 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AADP-ribosylation factor 1protein15538% helix, 22% strandP84080
EArnoprotein19362% helix, 1% strandQ99418

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · chains A
  • AFB · 1,6,7,8,9,11A,12,13,14,14A-decahydro-1,13-dihydroxy-6-methyl-4H-cyclopent[f]oxacyclotridecin-4-one · ligand · chains A, E
  • MG · Magnesium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14210.740.8452MG, AFB
2700.290.7319empty

Interfaces

1 interface between chains.

  • A–E · 1439 Ų buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (artifact).

Compared structures

  • 1S9D · ARF1[DELTA 1-17]-GDP-mg in complex with brefeldin a and a SEC7 domain · the same entry in another collection · chain E against E, TM-score 1.00
  • Q99418 · AlphaFold monomer V2.0 prediction for cytohesin-2 (Q99418) · a predicted model of the same protein · chain E against A, TM-score 0.90
  • P84080 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor 1 (P84080) · a predicted model of the same protein · chain A against A, TM-score 0.86

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