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Human pim-1 kinase in complex with an triazolo pyridazine inhibitor VX2

Analyse Human pim-1 kinase in complex with an triazolo pyridazine inhibitor VX2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BGQ
Type: protein
Length: 273 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proto-oncogene SERINE/THREONINE-protein kinase pim-1
EC: 2.7.11.1
UniProt: P11309
Ligands: VX2
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proto-oncogene SERINE/THREONINE-protein kinase pim-1 (EC 2.7.11.1)	protein	273	40% helix, 23% strand	P11309

Ligands and binding sites

VX2 · N-cyclohexyl-3-[3-(trifluoromethyl)phenyl][1,2,4]triazolo[4,3-b]pyridazin-6-amine · ligand · chains A

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

Pockets

2 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	342	0.69	0.82	42	VX2
2	51	0.30	0.76	13	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

3BGQ · Human Pim-1 kinase in complex with an triazolo pyridazine inhibitor VX2 · 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 P11309
Elsewhere: RCSB PDB 3BGQ · PDBe 3BGQ · UniProt P11309

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