Research workbench

Crystal structure of TGCDPK1 with inhibitor bound

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

PDB: 4IHP
Type: protein
Length: 454 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calmodulin-domain protein kinase 1
EC: 2.7.11.17
UniProt: Q9BJF5
Ligands: 1FB, UNX
Pockets: 4 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calmodulin-domain protein kinase 1 (EC 2.7.11.17)	protein	454	53% helix, 11% strand	Q9BJF5

Ligands and binding sites

1FB · 1-tert-butyl-3-(3-chlorophenoxy)-1H-pyrazolo[3,4-d]pyrimidin-4-amine · ligand · chains A
UNX · Unknown atom or ion · ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1148	0.84	0.85	124	1FB
2	125	0.39	0.74	23	empty
3	63	0.38	0.79	19	empty
4	58	0.32	0.76	13	empty

Compared structures

4IHP · Crystal structure of TgCDPK1 with inhibitor bound · 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 4IHP · PDBe 4IHP · UniProt Q9BJF5

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.