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CDPK1 from neospora caninum in complex with inhibitor rm-1-132

Analyse CDPK1 from neospora caninum in complex with inhibitor rm-1-132 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MXA
Type: protein
Length: 459 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calmodulin-like domain protein kinase isoenzyme gamma, related
EC: 2.7.11.17
UniProt: F0V9W9
Ligands: BK7
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calmodulin-like domain protein kinase isoenzyme gamma, related (EC 2.7.11.17)	protein	459	51% helix, 13% strand	F0V9W9

Ligands and binding sites

BK7 · 3-(6-ethoxynaphthalen-2-yl)-1-(piperidin-4-ylmethyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine · ligand · chains A

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

Pockets

3 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	1104	0.80	0.81	119	BK7
2	63	0.35	0.78	17	empty
3	65	0.32	0.76	16	empty

Compared structures

4MXA · CDPK1 from Neospora caninum in complex with inhibitor RM-1-132 · 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 F0V9W9
Elsewhere: RCSB PDB 4MXA · PDBe 4MXA · UniProt F0V9W9

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