MolNFT v1 · #27160 · protein

Crystal structure of the syk tyrosine kinase domain with staurosporin

1XBC · Tyrosine-protein kinase syk: “Crystal structure of the syk tyrosine kinase domain with staurosporin”. X-ray diffraction, 1 ligand (STU), 2 pockets (best druggability 0.62). MolNFT v1 #27160 on GenesisL1: 3D structure, binding sites…

PDB: 1XBC
Type: protein
Length: 268 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase syk
EC: 2.7.1.112
UniProt: P43405
Ligands: STU
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase syk (EC 2.7.1.112)	protein	268	41% helix, 24% strand	P43405

Ligands and binding sites

STU · Staurosporine · ligand · chains A

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

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	371	0.62	0.78	48	STU
2	52	0.25	0.72	13	empty

Compared structures

1XBC · Crystal structure of the syk tyrosine kinase domain with Staurosporin · the same entry in another collection · chain A against A, TM-score 1.00
P43405 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase syk (P43405) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 P43405
Elsewhere: RCSB PDB 1XBC · PDBe 1XBC · UniProt P43405

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