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Crystal structure of PHF2 phd domain complexed with H3K4ME3 peptide

Analyse Crystal structure of PHF2 phd domain complexed with H3K4ME3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3KQI
Type
protein
Length
77 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phd finger protein 2; H3K4ME3 peptide
UniProt
O75151, P68431
Ligands
ZN, MG, CL

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhd finger protein 2protein7120% helix, 17% strandO75151
BH3K4ME3 peptideprotein60% helix, 33% strandP68431

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A
  • MG · Magnesium ion · metal · 2 copies · chains A
  • CL · Chloride ion · ion · chains A
  • GOL · Glycerol · additive · chains A

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

Interfaces

1 interface between chains.

  • A–B · 524 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

  • 3KQI · crystal structure of PHF2 PHD domain complexed with H3K4Me3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • O75151 · AlphaFold monomer V2.0 prediction for lysine-specific demethylase PHF2 (O75151) · a predicted model of the same protein · chain A against A, TM-score 0.89

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