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Solution NMR structure of human BRD3 et complexed with NSD3(148-184) peptide

Analyse Solution NMR structure of human BRD3 et complexed with NSD3(148-184) peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7JYN
Type
protein
Length
135 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bromodomain-containing protein 3; Histone-lysine N-methyltransferase NSD3
EC
2.1.1.-
UniProt
Q15059, Q9BZ95

Structure

solution nmr · 2 distinct chains · 35% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABromodomain-containing protein 3protein9649% helix, 5% strandQ15059
BHistone-lysine N-methyltransferase NSD3 (EC 2.1.1.-)protein390% helix, 21% strandQ9BZ95

Interfaces

1 interface between chains.

  • A–B · 762 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 7JYN · Solution NMR structure of human Brd3 ET complexed with NSD3(148-184) peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • Q15059 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 3 (Q15059) · a predicted model of the same protein · chain A against A, TM-score 0.66
  • Q9BZ95 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase NSD3 (Q9BZ95) · a predicted model of the same protein · chain B against A, TM-score 0.34

Analyse

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