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Crystal structure of the human BRPF1 bromodomain in complex with SEED15

Analyse Crystal structure of the human BRPF1 bromodomain in complex with SEED15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EV9
Type: protein
Length: 112 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peregrin
UniProt: P55201
Ligands: 5SB, NO3
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peregrin	protein	112	66% helix, 0% strand	P55201

Ligands and binding sites

5SB · ~{N}-[5-(1~{H}-pyrazol-4-yl)quinolin-8-yl]ethanamide · ligand · chains A
NO3 · Nitrate ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	67	0.43	0.81	18	5SB

Compared structures

5EV9 · Crystal structure of the human BRPF1 bromodomain in complex with SEED15 · the same entry in another collection · chain A against A, TM-score 1.00
P55201 · AlphaFold monomer V2.0 prediction for peregrin (P55201) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P55201
Elsewhere: RCSB PDB 5EV9 · PDBe 5EV9 · UniProt P55201

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