Brand  (β version)

PDB ID: 3CQW

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Ligands
Code Name Style Show Link
CQW 5-(5-chloro-7h-pyrrolo[2,3-D]pyrimidin-4-yl)-4,5,6,7-tetrahydro-1h-imidazo[4,5-C]pyridine PoSSuM
MN Manganese (II) ion PoSSuM
Non-standard Residues
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TPO Phosphothreonine
Glycosylation
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Modification
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Structure summary

Code : 3CQW   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal Structure of Akt-1 complexed with substrate peptide and inhibitor
Release Data : 2008-05-27
Compound :
mol_id molecule chains synonym
1 RAC-alpha serine/threonine-protein kinase A RAC-PK-alpha, Protein kinase B, PKB, C-AKT
ec: 2.7.11.1
fragment: Kinase and AGC-kinase C-terminal domains
mutation: S473D
mol_id molecule chains synonym
2 Glycogen synthase kinase-3 beta C GSK-3 beta
ec: 2.7.11.26
fragment: residues 3-12
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Spodoptera frugiperda  (taxid:7108)
gene: AKT1, PKB, RAC
expression_system_common: Fall armyworm
expression_system_cell_line: Sf9
expression_system_vector_type: Baculovirus
mol_id organism_scientific organism_common
2 Homo sapiens  (taxid:9606) Human
synthetic: yes
Authors : Pandit, J.
Keywords : Kinase, Apoptosis, ATP-binding, Carbohydrate metabolism, Cytoplasm, Glucose metabolism, Glycogen biosynthesis, Glycogen metabolism, Membrane, Nucleotide-binding, Nucleus, Phosphoprotein, Serine/threonine-protein kinase, Sugar transport, Transferase, Translation regulation, Transport, Alternative splicing, Wnt signaling pathway
Exp. method : X-RAY DIFFRACTION ( 2.000 Å )
Citation :

Synthesis and structure based optimization of novel Akt inhibitors

Lippa, B.,Pan, G.,Corbett, M.  et al.
(2008)  Bioorg.Med.Chem.Lett.  18 : 3359 - 3363

PubMed: 18456494
DOI: 10.1016/j.bmcl.2008.04.034

Reaction

Chain : A
UniProt : P31749 (AKT1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+) 2.7.11.1 PubMed:12172553, PubMed:15861136, PubMed:16139227, PubMed:1718748, PubMed:1851997, PubMed:26440888, PubMed:29343641, PubMed:31548394, PubMed:32322062, PubMed:33594058
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+) 2.7.11.1 PubMed:12172553, PubMed:16139227, PubMed:1718748, PubMed:1851997
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Chain : C
UniProt : P49841 (GSK3B_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
L-seryl-[tau protein] + ATP = O-phospho-L-seryl-[tau protein] + ADP + H(+) 2.7.11.26 PubMed:14690523
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L-threonyl-[tau protein] + ATP = O-phospho-L-threonyl-[tau protein] + ADP + H(+) 2.7.11.26 PubMed:14690523
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+) 2.7.11.1 PubMed:17050006, PubMed:21343617, PubMed:22539723, PubMed:25827072, PubMed:28992046, PubMed:29059170
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+) 2.7.11.1 PubMed:17050006
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