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PDBsum entry 2zv2
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Transferase/transferase inhibitor
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PDB id
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2zv2
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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/transferase inhibitor
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Title:
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Crystal structure of human calcium/calmodulin-dependent protein kinase kinase 2, beta, camkk2 kinase domain in complex with sto-609
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Structure:
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Calcium/calmodulin-dependent protein kinase kinase 2. Chain: a. Fragment: kinase domain. Synonym: calcium/calmodulin-dependent protein kinase kinase beta, cam-kinase kinase beta, cam-kk beta, camkk beta. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: cell free protein synthesis.
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Resolution:
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2.40Å
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R-factor:
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0.203
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R-free:
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0.252
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Authors:
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S.Yoshikawa,M.Kukimoto-Niino,M.Shirouzu,A.Suzuki,S.Lee,Y.Minokoshi, S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
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Key ref:
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M.Kukimoto-Niino
et al.
(2011).
Crystal structure of the Ca²⁺/calmodulin-dependent protein kinase kinase in complex with the inhibitor STO-609.
J Biol Chem,
286,
22570-22579.
PubMed id:
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Date:
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31-Oct-08
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Release date:
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03-Nov-09
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PROCHECK
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Headers
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References
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Q96RR4
(KKCC2_HUMAN) -
Calcium/calmodulin-dependent protein kinase kinase 2 from Homo sapiens
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Seq:
Struc:
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588 a.a.
256 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:
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E.C.2.7.11.17
- calcium/calmodulin-dependent protein kinase.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[protein]
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+
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ADP
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+
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H(+)
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Cofactor:
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Ca(2+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Biol Chem
286:22570-22579
(2011)
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PubMed id:
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Crystal structure of the Ca²⁺/calmodulin-dependent protein kinase kinase in complex with the inhibitor STO-609.
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M.Kukimoto-Niino,
S.Yoshikawa,
T.Takagi,
N.Ohsawa,
Y.Tomabechi,
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
