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NMR solution structure of the phd domain from the yeast YNG1 protein in complex with H3(1-9)K4ME3 peptide

Analyse NMR solution structure of the phd domain from the yeast YNG1 protein in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2JMJ
Type
protein
Length
69 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein YNG1; Histone H3
UniProt
Q08465, P61830
Ligands
ZN

Structure

solution nmr · 2 distinct chains · 12% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein YNG1protein6013% helix, 10% strandQ08465
PHistone H3protein90% helix, 22% strandP61830

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A

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

Interfaces

1 interface between chains.

  • A–P · 598 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide, 1 modified (disulfide, methylation).

Compared structures

  • 2JMJ · NMR solution structure of the PHD domain from the yeast YNG1 protein in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q08465 · AlphaFold monomer V2.0 prediction for protein YNG1 (Q08465) · a predicted model of the same protein · chain A against A, TM-score 0.62
  • P61830 · AlphaFold monomer V2.0 prediction for histone H3 (P61830) · a predicted model of the same protein · chain P against A, TM-score 0.35

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