MolNFT v1 · #151625 · protein

Crystal structure of human btk SH2 domain bound to RF10 repebody

6HTF · Tyrosine-protein kinase btk: “Crystal structure of human btk SH2 domain bound to RF10 repebody”. X-ray diffraction, 2 pockets (best druggability 0.61). MolNFT v1 #151625 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6HTF
Type: protein
Length: 362 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase btk; RF10 repebody
EC: 2.7.10.2
UniProt: Q06187
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase btk (EC 2.7.10.2)	protein	104	18% helix, 26% strand	Q06187
B	RF10 repebody	protein	258	17% helix, 15% strand	—

Pockets

2 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	191	0.61	0.82	34	empty
2	83	0.34	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 1046 Å² buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6HTF · Crystal structure of human Btk SH2 domain bound to rF10 repebody · 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 A against A, TM-score 0.94

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 6HTF · PDBe 6HTF · UniProt Q06187

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