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Crystal structure of TGCDPK1 bound to NVPACU106

Analyse Crystal structure of TGCDPK1 bound to NVPACU106 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5JN2
Type: protein
Length: 450 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calmodulin-domain protein kinase 1
UniProt: Q9BJF5
Ligands: 6LO, CA
Pockets: 4 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calmodulin-domain protein kinase 1	protein	450	52% helix, 12% strand	Q9BJF5

Ligands and binding sites

6LO · N-[(3-{4-amino-5-[3-(benzyloxy)phenyl]-7H-pyrrolo[2,3-d]pyrimidin-7-yl}cyclobutyl)methyl]acetamide · ligand · chains A
CA · Calcium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 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	518	0.80	0.86	68	6LO
2	647	0.73	0.80	64	empty
3	193	0.61	0.83	27	empty
4	111	0.52	0.82	27	empty

Compared structures

5JN2 · Crystal structure of TgCDPK1 bound to NVPACU106 · 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 5JN2 · PDBe 5JN2 · UniProt Q9BJF5

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