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ATVAL1 phd-like domain in the P31 space group

Analyse ATVAL1 phd-like domain in the P31 space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5YUG
Type
protein
Length
388 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
B3 domain-containing transcription repressor VAL1
UniProt
Q8W4L5
Ligands
ZN
Pockets
4 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BB3 domain-containing transcription repressor VAL1protein9225% helix, 23% strandQ8W4L5
E, GB3 domain-containing transcription repressor VAL1protein10222% helix, 19% strandQ8W4L5

Ligands and binding sites

  • ZN · Zinc ion · metal · 12 copies · chains A, B, E, G
  • GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14000.700.8147empty
22140.610.8142GOL
31770.470.7634empty
4510.430.8320GOL

Interfaces

4 interfaces between chains.

  • B–E · 1322 Ų buried · 20 hydrogen bonds · protein-protein
  • B–G · 603 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 304 Ų buried · 0 hydrogen bonds · protein-protein
  • A–E · 189 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 5YUG · AtVAL1 PHD-Like domain in the P31 space group · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8W4L5 · AlphaFold monomer V2.0 prediction for B3 domain-containing transcription repressor VAL1… · a predicted model of the same protein · chain E against A, TM-score 0.97

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