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EDS1-PAD4 complexed with prib-ADP

Analyse EDS1-PAD4 complexed with prib-ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7XEY
Type
protein
Length
1,133 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein EDS1; Lipase-like PAD4
EC
2.3.1.-
UniProt
Q9SU72, Q9S745
Ligands
ADP, RP5
Pockets
13 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 59% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein EDS1protein61462% helix, 9% strandQ9SU72
BLipase-like PAD4 (EC 2.3.1.-)protein51956% helix, 10% strandQ9S745

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A, B
  • RP5 · 5-O-phosphono-beta-D-ribofuranose · ligand · chains A, B
  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A, B

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

Pockets

13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19340.830.8592empty
25540.830.8846ADP, RP5
3960.770.9826empty
44810.740.8353empty
52750.610.7942empty

Interfaces

1 interface between chains.

  • A–B · 3232 Ų buried · 37 hydrogen bonds · protein-protein

Compared structures

  • 7XEY · EDS1-PAD4 complexed with pRib-ADP · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9SU72 · AlphaFold monomer V2.0 prediction for protein EDS1 (Q9SU72) · a predicted model of the same protein · chain A against A, TM-score 0.99
  • Q9S745 · AlphaFold monomer V2.0 prediction for lipase-like PAD4 (Q9S745) · a predicted model of the same protein · chain B against A, TM-score 0.81

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