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Ligands
Code Name Style Show Link
CL Chloride ion
EDO 1,2-ethanediol
EPE 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid
JM1 Fluorinated pyridocarbazole cyclopentadienyl ru(co) complex
Non-standard Residues
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Glycosylation
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Code : 2OI4   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal structure of human PIM1 in complex with fluorinated ruthenium pyridocarbazole
Release Data : 2007-04-10
Compound :
mol_id molecule chains
1 Proto-oncogene serine/threonine-protein kinase Pim-1 X
ec: 2.7.11.1
mutation: R250G
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21  (taxid:511693)
gene: PIM1
expression_system_strain: BL21
expression_system_vector_type: Plasmid
expression_system_plasmid: pLIC-SGC1
Authors : Maksimoska, J., Meggers, E.
Keywords : TRANSFERASE, PIM1, Kinase, ATP-binding, Phosphorylation
Exp. method : X-RAY DIFFRACTION ( 2.20 Å )
Citation :

Ruthenium half-sandwich complexes as protein kinase inhibitors: derivatization of the pyridocarbazole pharmacophore ligand.

Pagano, N.,Maksimoska, J.,Bregman, H.  et al.
(2007)  Org.Biomol.Chem.  5 : 1218 - 1227

PubMed: 17406720
DOI: 10.1039/b700433h

Chain : X
UniProt : P11309 (PIM1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein] 2.7.11.1 PubMed:15525646, PubMed:15657054, PubMed:15808862, PubMed:31548394
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ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein] 2.7.11.1 PubMed:15525646, PubMed:15657054, PubMed:15808862
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