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PDBsum entry 3fe3
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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 the kinase mark3/par-1: t211a-s215a double mutant
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Structure:
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Map/microtubule affinity-regulating kinase 3. Chain: a, b. Fragment: catalytic and ubiquitin-associated domains, unp residues 41-367. Synonym: cdc25c-associated protein kinase 1, c-tak1, ctak1, serine/threonine protein kinase p78, ser/thr protein kinase par-1, protein kinase stk10. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: mark3. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.90Å
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R-factor:
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0.199
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R-free:
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0.233
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Authors:
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C.Nugoor,A.Marx,S.Panneerselvam,E.-M.Mandelkow,E.Mandelkow
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Key ref:
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C.Nugoor
et al.
Crystal structure of the kinase mark3/par-1: t211a-S215a double mutant.
To be published,
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Date:
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27-Nov-08
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Release date:
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16-Dec-08
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PROCHECK
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Headers
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References
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P27448
(MARK3_HUMAN) -
MAP/microtubule affinity-regulating kinase 3 from Homo sapiens
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Seq: Struc:
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753 a.a.
317 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 2 residue positions (black
crosses)
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Enzyme class:
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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]
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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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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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}
}
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