Structure of PDB 1yq3 Chain B Binding Site BS03

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 IDF3S
InChIInChI=1S/3Fe.4S
InChIKeyFCXHZBQOKRZXKS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385S1[Fe]S[Fe]2S[Fe]1S2
OpenEye OEToolkits 2.0.7S1[Fe]2S[Fe]3[S]2[Fe]1S3
FormulaFe3 S4
NameFE3-S4 CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain1yq3 Chain B Residue 1004 [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)		C168 Y178 P181 C215 T217 I218 M219 N220 C221
Binding residue
(residue number reindexed from 1)		C163 Y173 P176 C210 T212 I213 M214 N215 C216
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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