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Crystal structure of the anaplastic lymphoma kinase catalytic domain

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

PDB: 3LCT
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALK tyrosine kinase receptor
EC: 2.7.10.1
UniProt: Q9UM73
Ligands: ADP
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALK tyrosine kinase receptor (EC 2.7.10.1)	protein	308	42% helix, 15% strand	Q9UM73

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
GOL · Glycerol · additive · 2 copies · 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	464	0.65	0.77	45	ADP
2	51	0.30	0.76	14	GOL

Compared structures

3LCT · Crystal Structure of the Anaplastic Lymphoma Kinase Catalytic Domain · the same entry in another collection · chain A against A, TM-score 1.00
Q9UM73 · AlphaFold monomer V2.0 prediction for ALK tyrosine kinase receptor (Q9UM73) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9UM73
Elsewhere: RCSB PDB 3LCT · PDBe 3LCT · UniProt Q9UM73

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