MolNFT v1 · #117988 · protein

Crystal structure of human pim-1 kinase in complex with a macrocyclic quinoxaline-pyrrolodihydropiperidinone inhibitor

5EOL · SERINE/THREONINE-protein kinase pim-1: “Crystal structure of human pim-1 kinase in complex with a macrocyclic quinoxaline-pyrrolodihydropiperidinone…”. X-ray diffraction, 1 ligand (5QO), 2 pockets (best druggability 0.65). MolNFT v1…

PDB: 5EOL
Type: protein
Length: 273 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase pim-1
EC: 2.7.11.1
UniProt: P11309
Ligands: 5QO
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	SERINE/THREONINE-protein kinase pim-1 (EC 2.7.11.1)	protein	273	39% helix, 23% strand	P11309

Ligands and binding sites

5QO · macrocyclic quinoxaline-pyrrolodihydropiperidinone · ligand · chains A
GOL · Glycerol · additive · 2 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	226	0.65	0.83	24	5QO
2	132	0.51	0.81	28	empty

Compared structures

5EOL · Crystal structure of human Pim-1 kinase in complex with a macrocyclic… · 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 5EOL · PDBe 5EOL · UniProt P11309

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