GL1X · GenesisL1 explorer

Research workbench

Crystal structure of a human ANP32E-H2A.Z-H2B complex

Analyse Crystal structure of a human ANP32E-H2A.Z-H2B complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CAY
Type
protein
Length
201 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone H2A.Z; Histone H2B type 1-J; Acidic leucine-rich nuclear phosphoprotein 32 family…
UniProt
P0C0S5, P06899, Q9BTT0
Pockets
1 · best druggability 0.31

Structure

x-ray diffraction · 3 distinct chains · 68% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone H2A.Zprotein8673% helix, 3% strandP0C0S5
BHistone H2B type 1-Jprotein9275% helix, 4% strandP06899
CAcidic leucine-rich nuclear phosphoprotein 32 family member Eprotein2322% helix, 4% strandQ9BTT0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1540.310.7615empty

Interfaces

3 interfaces between chains.

  • A–B · 2636 Ų buried · 24 hydrogen bonds · protein-protein
  • B–C · 638 Ų buried · 9 hydrogen bonds · protein-protein
  • A–C · 611 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 4CAY · Crystal structure of a human Anp32e-H2A.Z-H2B complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P0C0S5 · AlphaFold monomer V2.0 prediction for histone H2A.Z (P0C0S5) · a predicted model of the same protein · chain A against A, TM-score 0.91
  • Q9BTT0 · AlphaFold monomer V2.0 prediction for acidic leucine-rich nuclear phosphoprotein 32… · a predicted model of the same protein · chain C against A, TM-score 0.23

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.