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Protein kinase pim-1 in complex with small molecule inibitor

Analyse Protein kinase pim-1 in complex with small molecule inibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XJ1
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, 2.7.11.1
UniProt: P11309
Ligands: XJ1
Pockets: 1 · best druggability 0.68

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, 2.7.11.1)	protein	274	39% helix, 23% strand	P11309

Ligands and binding sites

XJ1 · (2E)-3-(3-{6-[(trans-4-aminocyclohexyl)amino]pyrazin-2-yl}phenyl)prop-2-enoic acid · 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	326	0.68	0.82	44	XJ1

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

2XJ1 · Protein kinase Pim-1 in complex with small molecule inibitor · 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 2XJ1 · PDBe 2XJ1 · UniProt P11309

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