Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
0FN 1,3-dioxo-2,3-dihydro-1h-indene-2-carbonitrile
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 3VBW   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/TRANSFERASE INHIBITOR
Title : Exploitation of hydrogen bonding constraints and flat hydrophobic energy landscapes in Pim-1 kinase needle screening and inhibitor design
Release Data : 2012-03-21
Compound :
mol_id molecule chains
1 Serine/threonine-protein kinase pim-1 A
ec: 2.7.11.1
fragment: unp residues 120-404
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: PIM1
Authors : Liu, J.
Keywords : Pim1, TRANSFERASE-TRANSFERASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.48 Å )
Citation :

Implications of promiscuous Pim-1 kinase fragment inhibitor hydrophobic interactions for fragment-based drug design.

Good, A.C.,Liu, J.,Hirth, B.  et al.
(2012)  J.Med.Chem.  55 : 2641 - 2648

PubMed: 22339127
DOI: 10.1021/jm2014698

Chain : A
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
-
ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein] 2.7.11.1 PubMed:15525646, PubMed:15657054, PubMed:15808862
-