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Crystal structure of BRUTON'S tyrosine kinase domain

Analyse Crystal structure of BRUTON'S tyrosine kinase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1K2P
Type: protein
Length: 516 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase btk
EC: 2.7.1.112
UniProt: Q06187
Pockets: 4 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tyrosine-protein kinase btk (EC 2.7.1.112)	protein	258	38% helix, 16% strand	Q06187

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	995	0.85	0.86	119	empty
2	380	0.80	0.89	47	empty
3	61	0.42	0.82	16	empty
4	83	0.37	0.77	16	empty

Interfaces

1 interface between chains.

A–B · 1064 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

1K2P · Crystal structure of Bruton's tyrosine kinase domain · the same entry in another collection · chain A against A, TM-score 1.00
Q06187 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase btk (Q06187) · a predicted model of the same protein · chain B against A, TM-score 0.91

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 1K2P · PDBe 1K2P · UniProt Q06187

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