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Crystal structure of human HBO1-BRPF2 in complex with propionyl-coenzyme A

Analyse Crystal structure of human HBO1-BRPF2 in complex with propionyl-coenzyme A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7D0P
Type
protein
Length
304 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.8
Source
Homo sapiens
Molecule
Histone acetyltransferase KAT7; BRD1 protein
EC
2.3.1.48
UniProt
O95251, Q86X06
Ligands
1VU, ZN, CL
Pockets
3 · best druggability 0.69

Structure

x-ray diffraction · resolution 1.8 · 2 distinct chains · 34% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone acetyltransferase KAT7 (EC 2.3.1.48)protein27637% helix, 26% strandO95251
BBRD1 proteinprotein280% helix, 57% strandQ86X06

Ligands and binding sites

  • 1VU · propionyl Coenzyme A · ligand · chains A
  • ZN · Zinc ion · metal · chains A
  • CL · Chloride ion · ion · chains B

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13320.690.83381VU
2620.480.8521empty
31430.440.7620empty

Interfaces

1 interface between chains.

  • A–B · 984 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

  • 7D0P · Crystal structure of human HBO1-BRPF2 in complex with propionyl- coenzyme a · the same entry in another collection · chain A against A, TM-score 1.00
  • O95251 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT7 (O95251) · a predicted model of the same protein · chain A against A, TM-score 0.98

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