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Crystal structure of kinase PIM1 in complex with 3,4-dihydroxy-1- methylquinolin-2(1H)-one

Analyse Crystal structure of kinase PIM1 in complex with 3,4-dihydroxy-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YXV
Type: protein
Length: 274 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: 2.7.1.37
UniProt: P11309
Ligands: LI6
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proto-oncogene SERINE/THREONINE-protein kinase pim-1 (EC 2.7.1.37)	protein	274	39% helix, 23% strand	P11309

Ligands and binding sites

LI6 · 3,4-dihydroxy-1-methylquinolin-2(1H)-one · ligand · chains A
IMD · Imidazole · additive · 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	205	0.65	0.84	26	LI6
2	109	0.45	0.79	25	empty

Compared structures

1YXV · Crystal Structure of Kinase Pim1 in complex with 3,4-Dihydroxy-1-methylquinolin-2(1H)-one · 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 1YXV · PDBe 1YXV · UniProt P11309

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