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PDBsum entry 2yza
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Transferase
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Title:
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Crystal structure of kinase domain of human 5'-amp-activated protein kinase alpha-2 subunit mutant (t172d)
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Structure:
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5'-amp-activated protein kinase catalytic subunit alpha-2. Chain: a. Fragment: kinase domain. Synonym: 5'-amp-activated protein kinase alpha-2 subunit, ampk alpha- 2 chain. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: prkaa2, ampk, ampk2. Expressed in: cell-free protein synthesis.
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Resolution:
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3.02Å
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R-factor:
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0.235
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R-free:
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0.308
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Authors:
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S.Saijo,T.Takagi,S.Yoshikawa,S.Kishishita,M.Shirouzu,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
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Key ref:
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N.Handa
et al.
(2011).
Structural basis for compound C inhibition of the human AMP-activated protein kinase α2 subunit kinase domain.
Acta Crystallogr D Biol Crystallogr,
67,
480-487.
PubMed id:
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Date:
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04-May-07
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Release date:
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06-May-08
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PROCHECK
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Headers
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References
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P54646
(AAPK2_HUMAN) -
5'-AMP-activated protein kinase catalytic subunit alpha-2 from Homo sapiens
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Seq:
Struc:
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552 a.a.
258 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class 2:
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E.C.2.7.11.27
- Transferred entry: 2.7.11.31.
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Reaction:
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ATP + L-seryl-[acetyl-CoA carboxylase] = ADP + H+ + O-phospho-L-seryl- [acetyl-CoA carboxylase]
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ATP
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+
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L-seryl-[acetyl-CoA carboxylase]
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=
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ADP
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+
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H(+)
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+
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O-phospho-L-seryl- [acetyl-CoA carboxylase]
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Enzyme class 3:
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E.C.2.7.11.31
- [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase.
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Reaction:
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L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase] + ATP = O-phospho-L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase] + ADP + H+
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L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase]
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+
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ATP
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=
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O-phospho-L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase]
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+
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ADP
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Acta Crystallogr D Biol Crystallogr
67:480-487
(2011)
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PubMed id:
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Structural basis for compound C inhibition of the human AMP-activated protein kinase α2 subunit kinase domain.
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N.Handa,
T.Takagi,
S.Saijo,
S.Kishishita,
D.Takaya,
M.Toyama,
T.Terada,
M.Shirouzu,
A.Suzuki,
S.Lee,
T.Yamauchi,
M.Okada-Iwabu,
M.Iwabu,
T.Kadowaki,
Y.Minokoshi,
S.Yokoyama.
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ABSTRACT
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Links
