Structure of PDB 1yq3 Chain B Binding Site BS01

Receptor Information
>1yq3 Chain B (length=242) Species: 9031 (Gallus gallus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AATSRIKKFSIYRWDPDKPGDKPRMQTYEVDLNKCGPMVLDALIKIKNEL
DSTLTFRRSCREGICGSCAMNIAGGNTLACTKKIDPDLSKTTKIYPLPHM
YVVKDLVPDLSNFYAQYKSIEPYLKKKDESKQGKEQYLQSIEDRQKLDGL
YECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDYTEERLAQ
LQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMATYKE
Ligand information
Ligand IDFES
InChIInChI=1S/2Fe.2S
InChIKeyNIXDOXVAJZFRNF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04[Fe]1S[Fe]S1
CACTVS 3.341
OpenEye OEToolkits 1.5.0
S1[Fe]S[Fe]1
FormulaFe2 S2
NameFE2/S2 (INORGANIC) CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain1yq3 Chain B Residue 1002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1yq3 3-Nitropropionic Acid Is a Suicide Inhibitor of Mitochondrial Respiration That, upon Oxidation by Complex II, Forms a Covalent Adduct with a Catalytic Base Arginine in the Active Site of the Enzyme
Resolution2.2 Å
Binding residue
(original residue number in PDB)
C65 R66 G68 C70 G71 S72 C73 C85
Binding residue
(residue number reindexed from 1)
C60 R61 G63 C65 G66 S67 C68 C80
Annotation score1
Enzymatic activity
Enzyme Commision number 1.3.5.1: succinate dehydrogenase.
Gene Ontology
Molecular Function
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0051536 iron-sulfur cluster binding
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0006099 tricarboxylic acid cycle

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Molecular Function

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Biological Process
External links
PDB RCSB:1yq3, PDBe:1yq3, PDBj:1yq3
PDBsum1yq3
PubMed16371358
UniProtQ9YHT2|SDHB_CHICK Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (Gene Name=SDHB)

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