Research workbench

The pH domain of BRUTON'S tyrosine kinase mutant R28C

Analyse The pH domain of BRUTON'S tyrosine kinase mutant R28C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6TT2
Type: protein
Length: 324 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q06187
Ligands: MG, ZN

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	164	—	Q06187
B	—	protein	160	—	Q06187

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies
ZN · Zinc ion · metal · 2 copies · chains A, B

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

Compared structures

6TT2 · The PH domain of Bruton's tyrosine kinase mutant R28C · 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 0.97

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 6TT2 · PDBe 6TT2 · UniProt Q06187

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