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PDBsum entry 3vrb
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Oxidoreductase/oxidoreductase inhibitor
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PDB id
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3vrb
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Contents |
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613 a.a.
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249 a.a.
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153 a.a.
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129 a.a.
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PDB id:
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| Name: |
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Oxidoreductase/oxidoreductase inhibitor
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Title:
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Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode ascaris suum with the specific inhibitor flutolanil and substrate fumarate
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Structure:
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Flavoprotein subunit of complex ii. Chain: a, e. Synonym: rhodoquinol-fumarate reductase fp subunit. Iron-sulfur subunit of succinate dehydrogenase. Chain: b, f. Synonym: rhodoquinol-fumarate reductase ip subunit. Cytochrome b-large subunit. Chain: c, g. Synonym: rhodoquinol-fumarate reductase cybl subunit.
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Source:
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Ascaris suum. Pig roundworm. Organism_taxid: 6253. Organelle: mitochondria. Other_details: adult. Other_details: adult
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Resolution:
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2.91Å
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R-factor:
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0.207
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R-free:
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0.272
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Authors:
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H.Shimizu,T.Shiba,D.K.Inaoka,A.Osanai,K.Kita,K.Sakamoto,S.Harada
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Key ref:
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H.Shimizu
et al.
(2012).
Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum.
J Biochem (tokyo),
151,
589-592.
PubMed id:
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Date:
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07-Apr-12
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Release date:
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11-Jul-12
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PROCHECK
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Headers
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References
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Q33862
(SDHA1_ASCSU) -
Succinate dehydrogenase [rhodoquinone] flavoprotein subunit 1, mitochondrial from Ascaris suum
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Seq:
Struc:
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645 a.a.
613 a.a.
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O44074
(SDHB_ASCSU) -
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial from Ascaris suum
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Seq:
Struc:
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282 a.a.
249 a.a.
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Enzyme class:
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Chains A, B, E, F:
E.C.1.3.5.1
- succinate dehydrogenase.
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Pathway:
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Citric acid cycle
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Reaction:
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a quinone + succinate = fumarate + a quinol
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quinone
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+
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succinate
Bound ligand (Het Group name = )
corresponds exactly
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=
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fumarate
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+
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quinol
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Cofactor:
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FAD; Iron-sulfur
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FAD
Bound ligand (Het Group name =
FAD)
corresponds exactly
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Iron-sulfur
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Biochem (tokyo)
151:589-592
(2012)
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PubMed id:
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Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum.
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H.Shimizu,
A.Osanai,
K.Sakamoto,
D.K.Inaoka,
T.Shiba,
S.Harada,
K.Kita.
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ABSTRACT
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