Research workbench

Lyn tyrosine kinase domain-PP2 complex

Analyse Lyn tyrosine kinase domain-PP2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZV9
Type: protein
Length: 256 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase lyn
EC: 2.7.10.2
UniProt: P25911
Ligands: PP2
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase lyn (EC 2.7.10.2)	protein	256	38% helix, 17% strand	P25911

Ligands and binding sites

PP2 · 1-tert-butyl-3-(4-chloro-phenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	504	0.69	0.79	47	PP2

Compared structures

2ZV9 · Lyn Tyrosine Kinase Domain-PP2 complex · the same entry in another collection · chain A against A, TM-score 1.00
P25911 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase lyn (P25911) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P25911
Elsewhere: RCSB PDB 2ZV9 · PDBe 2ZV9 · UniProt P25911

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