Research workbench

BRD4-BD2 in complex with the cyclic peptide 3.2_2

Analyse BRD4-BD2 in complex with the cyclic peptide 3.2_2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6U8I
Type: protein
Length: 121 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bromodomain-containing protein 4; Cyclic peptide 3.2_2
UniProt: O60885
Ligands: ACE, NH2

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bromodomain-containing protein 4	protein	109	71% helix, 0% strand	O60885
B	Cyclic peptide 3.2_2	protein	12	75% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains B
NH2 · Amino group · ion · chains B

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

Interfaces

1 interface between chains.

A–B · 636 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent, 1 modified (covalent ligand, acetylation).

Compared structures

6U8I · BRD4-BD2 in complex with the cyclic peptide 3.2_2 · 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 0.98

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
Elsewhere: RCSB PDB 6U8I · PDBe 6U8I · UniProt O60885

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