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Crystal structure of fyn kinase domain complexed with staurosporine

Analyse Crystal structure of fyn kinase domain complexed with staurosporine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2DQ7
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proto-oncogene tyrosine-protein kinase fyn
EC: 2.7.10.2
UniProt: P06241
Ligands: STU
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Proto-oncogene tyrosine-protein kinase fyn (EC 2.7.10.2)	protein	263	35% helix, 19% strand	P06241

Ligands and binding sites

STU · Staurosporine · ligand · chains X

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	385	0.67	0.80	45	STU

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

2DQ7 · Crystal Structure of Fyn kinase domain complexed with staurosporine · the same entry in another collection · chain X against X, TM-score 1.00
P06241 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase fyn (P06241) · a predicted model of the same protein · chain X 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 P06241
Elsewhere: RCSB PDB 2DQ7 · PDBe 2DQ7 · UniProt P06241

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