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The complex crystal structure of lck with a probe molecule W259

Analyse The complex crystal structure of lck with a probe molecule W259 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KXZ
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proto-oncogene tyrosine-protein kinase lck
EC: 2.7.10.2
UniProt: P06239
Ligands: 925, CA, SO4
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proto-oncogene tyrosine-protein kinase lck (EC 2.7.10.2)	protein	264	39% helix, 19% strand	P06239

Ligands and binding sites

925 · 3-[7-[(3-hydroxyphenyl)amino]pyrazolo[1,5-a]pyrimidin-2-yl]-N-(1-hydroxy-2,2,6,6-tetramethyl-piperidin-4-yl)benzamide · ligand · chains A
CA · Calcium ion · metal · chains A
SO4 · Sulfate ion · ion · 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	430	0.67	0.79	49	925

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

3KXZ · The complex crystal structure of LCK with a probe molecule w259 · the same entry in another collection · chain A against A, TM-score 1.00

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 P06239
Elsewhere: RCSB PDB 3KXZ · PDBe 3KXZ · UniProt P06239

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