MolNFT v1 · #45774 · protein

Solution NMR structures of BRD4 et domain in complex with NSD3_3 peptide

2ND1 · Bromodomain-containing protein 4: “Solution NMR structures of BRD4 et domain in complex with NSD3_3 peptide”. Solution nmr. MolNFT v1 #45774 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2ND1
Type: protein
Length: 96 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bromodomain-containing protein 4; Histone-lysine N-methyltransferase NSD3
EC: 2.1.1.43
UniProt: O60885, Q9BZ95

Structure

solution nmr · 2 distinct chains · 49% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bromodomain-containing protein 4	protein	83	57% helix, 2% strand	O60885
B	Histone-lysine N-methyltransferase NSD3 (EC 2.1.1.43)	protein	13	0% helix, 15% strand	Q9BZ95

Interfaces

1 interface between chains.

A–B · 797 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

2ND1 · Solution NMR structures of BRD4 ET domain in complex with NSD3_3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
O60885 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 4 (O60885) · a predicted model of the same protein · chain A against A, TM-score 0.81
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 0.24

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O60885
Every structure of UniProt Q9BZ95
Elsewhere: RCSB PDB 2ND1 · PDBe 2ND1 · UniProt O60885 · UniProt Q9BZ95

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