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Structure of bromodomain from human BAZ1A

Analyse Structure of bromodomain from human BAZ1A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UIY
Type: protein
Length: 423 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9NRL2

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	107	—	Q9NRL2
B	—	protein	107	—	Q9NRL2
C	—	protein	106	—	Q9NRL2
D	—	protein	103	—	Q9NRL2

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B, C, D

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

Compared structures

5UIY · Structure of Bromodomain from human BAZ1A · the same entry in another collection · chain D against D, TM-score 1.00
Q9NRL2 · AlphaFold monomer V2.0 prediction for bromodomain adjacent to zinc finger domain protein… · a predicted model of the same protein · chain D against A, TM-score 0.99

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 Q9NRL2
Elsewhere: RCSB PDB 5UIY · PDBe 5UIY · UniProt Q9NRL2

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