Research workbench

Crystal structure of human PIM1 in complex with imidazopyridazin I

Analyse Crystal structure of human PIM1 in complex with imidazopyridazin I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2C3I
Type: protein
Length: 274 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pimtide; Proto-oncogene serine threonine protein kinase PIM1
EC: 2.7.1.37
UniProt: P11309
Ligands: IYZ
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pimtide	protein	8	0% helix, 0% strand	—
B	Proto-oncogene serine threonine protein kinase PIM1 (EC 2.7.1.37)	protein	266	39% helix, 23% strand	P11309

Ligands and binding sites

IYZ · 1-(3-{6-[(cyclopropylmethyl)amino]imidazo[1,2-b]pyridazin-3-yl}phenyl)ethanone · ligand · chains B

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	431	0.71	0.82	54	IYZ

Interfaces

1 interface between chains.

A–B · 578 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

2C3I · Crystal structure of human PIM1 in complex with imidazopyridazin I · 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 2C3I · PDBe 2C3I · UniProt P11309

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.