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Crystal structure of phd finger-linker-bromodomain fragment of human bptf in the H3(1-15)K4ME3 bound state

Analyse Crystal structure of phd finger-linker-bromodomain fragment of human bptf in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2F6J
Type
protein
Length
507 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bromodomain phd finger transcription factor; Histone H3, N-terminal
UniProt
Q7Z7D6
Ligands
ZN
Pockets
4 · best druggability 0.54

Structure

x-ray diffraction · 4 distinct chains · 51% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABromodomain phd finger transcription factorprotein16852% helix, 6% strandQ7Z7D6
BBromodomain phd finger transcription factorprotein16751% helix, 8% strandQ7Z7D6
CBromodomain phd finger transcription factorprotein16654% helix, 8% strandQ7Z7D6
PHistone H3, N-terminalprotein60% helix, 33% strand—

Ligands and binding sites

  • ZN · Zinc ion · metal · 6 copies · chains A, B, C

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
12970.540.7533empty
2980.500.8218empty
31060.500.8120empty
41000.490.8121empty

Interfaces

3 interfaces between chains.

  • A–P · 540 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 524 Ų buried · 11 hydrogen bonds · protein-protein
  • A–B · 30 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered, methylation).

Compared structures

  • 2F6J · Crystal structure of PHD finger-linker-bromodomain fragment of human BPTF in the… · the same entry in another collection · chain A against A, TM-score 1.00

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