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Crystal structure of human ASH2L (spry domain and sdi motif) in complex with full length dpy-30

Analyse Crystal structure of human ASH2L (spry domain and sdi motif) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6E2H
Type
protein
Length
311 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SET1/ASH2 histone methyltransferase complex subunit ASH2; Protein dpy-30 homolog
UniProt
Q9UBL3, Q9C005

Structure

x-ray diffraction · 3 distinct chains · 31% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
DSET1/ASH2 histone methyltransferase complex subunit ASH2protein21412% helix, 39% strandQ9UBL3
EProtein dpy-30 homologprotein4779% helix, 0% strandQ9C005
FProtein dpy-30 homologprotein5070% helix, 0% strandQ9C005

Interfaces

1 interface between chains.

  • E–F · 1157 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 6E2H · Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length… · the same entry in another collection · chain D against D, TM-score 1.00
  • Q9C005 · AlphaFold monomer V2.0 prediction for protein dpy-30 homolog (Q9C005) · a predicted model of the same protein · chain F against A, TM-score 0.97
  • Q9UBL3 · AlphaFold monomer V2.0 prediction for SET1/ASH2 histone methyltransferase complex subunit… · a predicted model of the same protein · chain D against A, TM-score 0.86

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