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Solution NMR structures of BRD4 et domain with JMJD6 peptide

Analyse Solution NMR structures of BRD4 et domain with JMJD6 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BNH
Type: protein
Length: 96 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bromodomain-containing protein 4; Bifunctional arginine demethylase and lysyl-hydroxylase…
EC: 1.14.11.-
UniProt: O60885, Q6NYC1

Structure

solution nmr · 2 distinct chains · 57% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bromodomain-containing protein 4	protein	83	59% helix, 0% strand	O60885
B	Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-)	protein	13	46% helix, 0% strand	Q6NYC1

Interfaces

1 interface between chains.

A–B · 776 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6BNH · Solution NMR structures of BRD4 ET domain with JMJD6 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 0.80
Q6NYC1 · AlphaFold monomer V2.0 prediction for bifunctional arginine demethylase and… · a predicted model of the same protein · chain B against A, TM-score 0.40

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 Q6NYC1
Elsewhere: RCSB PDB 6BNH · PDBe 6BNH · UniProt O60885 · UniProt Q6NYC1

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