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PDBsum entry 4tle
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PDB id:
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Transferase
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Title:
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Crystal structure of n-terminal c1 domain of kaic
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Structure:
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Circadian clock protein kinase kaic. Chain: a, b, c, d, e, f. Fragment: n-terminal domain, residues 1-253. Engineered: yes. Mutation: yes
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Source:
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Synechococcus elongatus pcc 7942. Organism_taxid: 1140. Strain: pcc 7942. Gene: kaic, synpcc7942_1216, see0011. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.94Å
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R-factor:
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0.191
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R-free:
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0.229
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Authors:
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J.Abe,T.B.Hiyama,A.Mukaiyama,S.Son,S.Akiyama
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Key ref:
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J.Abe
et al.
(2015).
Circadian rhythms. Atomic-scale origins of slowness in the cyanobacterial circadian clock.
Science,
349,
312-316.
PubMed id:
DOI:
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Date:
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29-May-14
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Release date:
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01-Jul-15
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PROCHECK
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Headers
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References
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Q79PF4
(KAIC_SYNE7) -
Circadian clock oscillator protein KaiC from Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
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Seq:
Struc:
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519 a.a.
218 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class 1:
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E.C.2.7.11.1
- non-specific serine/threonine 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]
Bound ligand (Het Group name = )
matches with 93.75% similarity
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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]
Bound ligand (Het Group name = )
matches with 93.75% similarity
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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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Enzyme class 2:
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E.C.3.6.4.-
- ?????
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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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DOI no:
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Science
349:312-316
(2015)
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PubMed id:
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Circadian rhythms. Atomic-scale origins of slowness in the cyanobacterial circadian clock.
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J.Abe,
T.B.Hiyama,
A.Mukaiyama,
S.Son,
T.Mori,
S.Saito,
M.Osako,
J.Wolanin,
E.Yamashita,
T.Kondo,
S.Akiyama.
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ABSTRACT
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Links
