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Crystal structure of TGCDPK1 bound to CGP060476

Analyse Crystal structure of TGCDPK1 bound to CGP060476 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5JMS
Type: protein
Length: 447 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calmodulin-domain protein kinase 1
UniProt: Q9BJF5
Ligands: 6LP, CA
Pockets: 4 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calmodulin-domain protein kinase 1	protein	447	53% helix, 13% strand	Q9BJF5

Ligands and binding sites

6LP · N~1~-(4-{2-[(3-chlorophenyl)amino]pyrimidin-4-yl}pyridin-2-yl)ethane-1,2-diamine · ligand · chains A
CA · Calcium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1110	0.80	0.81	120	6LP
2	72	0.71	0.96	15	empty
3	147	0.56	0.82	21	empty
4	137	0.52	0.81	37	empty

Compared structures

5JMS · Crystal structure of TgCDPK1 bound to CGP060476 · 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 Q9BJF5
Elsewhere: RCSB PDB 5JMS · PDBe 5JMS · UniProt Q9BJF5

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