MolNFT v1 · #28559 · protein

Crystal structure of pim-1 bound to LY294002

1YI3 · Proto-oncogene SERINE/THREONINE-protein kinase pim-1: “Crystal structure of pim-1 bound to LY294002”. X-ray diffraction, 1 ligand (LY2), 1 pocket (best druggability 0.67). MolNFT v1 #28559 on GenesisL1: 3D structure, binding sites…

PDB: 1YI3
Type: protein
Length: 269 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: LY2
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 41% 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	269	41% helix, 23% strand	P11309

Ligands and binding sites

LY2 · 2-morpholin-4-yl-7-phenyl-4H-chromen-4-one · ligand · 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	363	0.67	0.81	47	LY2

Modifications

Observed in the structure: 2 modified (artifact, phosphorylation).

Compared structures

1YI3 · Crystal Structure of Pim-1 bound to LY294002 · 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 1YI3 · PDBe 1YI3 · UniProt P11309

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