MolNFT v1 · #122450 · protein

Crystal structure of human pim-1 kinase in complex with a quinazolinone-pyrrolopyrrolone inhibitor.

5IPJ · SERINE/THREONINE-protein kinase pim-1: “Crystal structure of human pim-1 kinase in complex with a quinazolinone-pyrrolopyrrolone inhibitor.”. X-ray diffraction, 1 ligand (6CD), 1 pocket (best druggability 0.69). MolNFT v1 #122450 on…

PDB: 5IPJ
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: 6CD
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 40% 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	40% helix, 23% strand	P11309

Ligands and binding sites

6CD · 2-(tert-butylamino)-3-methyl-8-[(6R)-6-methyl-4-oxo-1,4,5,6-tetrahydropyrrolo[3,4-b]pyrrol-2-yl]quinazolin-4(3H)-one · ligand · chains A
GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	369	0.69	0.82	50	6CD

Compared structures

5IPJ · Crystal structure of human Pim-1 kinase in complex with a quinazoli -pyrrolopyrrolone… · 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 5IPJ · PDBe 5IPJ · UniProt P11309

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