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The kinase domain of human lymphocyte kinase (lck), activated form (auto-phosphorylated on TYR394)

Analyse The kinase domain of human lymphocyte kinase (lck), activated form… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LCK
Type: protein
Length: 271 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proto-oncogene tyrosine-protein kinase
EC: 2.7.1.112
UniProt: P06239
Ligands: SO4
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proto-oncogene tyrosine-protein kinase (EC 2.7.1.112)	protein	271	38% helix, 20% strand	P06239

Ligands and binding sites

SO4 · Sulfate ion · ion · 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	334	0.60	0.77	36	empty
2	50	0.32	0.77	13	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

3LCK · The kinase domain of human lymphocyte kinase (lck), activated form (auto-phosphorylated… · 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 3LCK · PDBe 3LCK · UniProt P06239

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