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PDBsum entry 4j2t
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Hydrolase/hydrolase inhibitor
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PDB id
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4j2t
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PDB id:
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| Name: |
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Hydrolase/hydrolase inhibitor
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Title:
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Inhibitor-bound ca2+ atpase
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Structure:
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Serca1a. Chain: a. Ec: 3.6.3.8
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Source:
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Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Tissue: fast twitch skeletal muscle
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Resolution:
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3.20Å
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R-factor:
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0.262
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R-free:
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0.286
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Authors:
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E.S.Paulsen,J.Villadsen,E.Tenori,H.Liu,M.A.Lie,D.F.Bonde,M.Bublitz, C.Olesen,H.E.Autzen,I.Dach,P.Sehgal,J.V.Moller,B.Schiott,P.Nissen, S.B.Christensen
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Key ref:
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E.S.Paulsen
et al.
(2013).
Water-mediated interactions influence the binding of thapsigargin to sarco/endoplasmic reticulum calcium adenosinetriphosphatase.
J Med Chem,
56,
3609-3619.
PubMed id:
DOI:
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Date:
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05-Feb-13
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Release date:
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19-Jun-13
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PROCHECK
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Headers
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References
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P04191
(AT2A1_RABIT) -
Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 from Oryctolagus cuniculus
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Seq:
Struc:
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1001 a.a.
994 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:
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E.C.7.2.2.10
- P-type Ca(2+) transporter.
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Reaction:
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Ca2+(in) + ATP + H2O = Ca2+(out) + ADP + phosphate + H+
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Ca(2+)(in)
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+
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ATP
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+
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H2O
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=
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Ca(2+)(out)
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+
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ADP
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+
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phosphate
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+
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H(+)
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Cofactor:
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Mg(2+)
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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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J Med Chem
56:3609-3619
(2013)
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PubMed id:
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Water-mediated interactions influence the binding of thapsigargin to sarco/endoplasmic reticulum calcium adenosinetriphosphatase.
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E.S.Paulsen,
J.Villadsen,
E.Tenori,
H.Liu,
D.F.Bonde,
M.A.Lie,
M.Bublitz,
C.Olesen,
H.E.Autzen,
I.Dach,
P.Sehgal,
P.Nissen,
J.V.Møller,
B.Schiøtt,
S.B.Christensen.
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ABSTRACT
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A crystal structure suggests four water molecules are present in the binding
cavity of thapsigargin in sarco/endoplasmic reticulum calcium ATPase (SERCA).
Computational chemistry indicates that three of these water molecules mediate an
extensive hydrogen-bonding network between thapsigargin and the backbone of
SERCA. The orientation of the thapsigargin molecule in SERCA is crucially
dependent on these interactions. The hypothesis has been verified by measuring
the affinity of newly synthesized model compounds, which are prevented from
participating in such water-mediated interactions as hydrogen-bond donors.
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