Research workbench

BTK1 in complex with cc 292

Analyse BTK1 in complex with cc 292 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5P9L
Type: protein
Length: 252 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase btk
EC: 2.7.10.2
UniProt: Q06187
Ligands: 7G9
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase btk (EC 2.7.10.2)	protein	252	43% helix, 16% strand	Q06187

Ligands and binding sites

7G9 · ~{N}-[3-[[5-fluoranyl-2-[[4-(2-methoxyethoxy) phenyl]amino]pyrimidin-4-yl]amino]phenyl]propanamide · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	376	0.64	0.79	39	7G9
2	52	0.46	0.84	14	empty
3	106	0.38	0.74	19	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

Q06187 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase btk (Q06187) · 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 Q06187
Elsewhere: RCSB PDB 5P9L · PDBe 5P9L · UniProt Q06187

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.