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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: 4IFG
Type: protein
Length: 452 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: 1E8, UNX
Pockets: 4 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calmodulin-domain protein kinase 1 (EC 2.7.11.17)	protein	452	54% helix, 12% strand	Q9BJF5

Ligands and binding sites

1E8 · 1-{(3R)-3-[4-amino-3-(4-phenoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-1-yl]piperidin-1-yl}prop-2-en-1-one · ligand · chains A
UNX · Unknown atom or ion · ion · 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	1150	0.84	0.85	121	1E8
2	82	0.38	0.77	19	empty
3	80	0.35	0.75	15	empty
4	52	0.32	0.78	18	empty

Compared structures

4IFG · 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 4IFG · PDBe 4IFG · UniProt Q9BJF5

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