Structure of PDB 2fyn Chain R Binding Site BS01

Receptor Information
>2fyn Chain R (length=179) Species: 1063 (Cereibacter sphaeroides) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GTRRDFLYYATAGAGAVATGAAVWPLINQMNPSADVQALASIFVDVSSVE
PGVQLTVKFLGKPIFIRRRTEADIELGRSVQLGQLVDTNARNANIDAGAE
ATDQNRTLDEAGEWLVMWGVCTHLGCSPIGGVSGDFGGWFCPCHGSHYDS
AGRIRKGPAPENLPIPLAKFIDETTIQLG
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 chain2fyn Chain R Residue 200 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2fyn Surface-modulated motion switch: Capture and release of iron-sulfur protein in the cytochrome bc1 complex.
Resolution3.2 Å
Binding residue
(original residue number in PDB)		C129 H131 L132 C134 C149 C151 H152 S154
Binding residue
(residue number reindexed from 1)		C121 H123 L124 C126 C141 C143 H144 S146
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H152
Catalytic site (residue number reindexed from 1) H144
Enzyme Commision number 7.1.1.8: quinol--cytochrome-c reductase.
Gene Ontology
Molecular Function
GO:0008121 ubiquinol-cytochrome-c reductase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2fyn, PDBe:2fyn, PDBj:2fyn
PDBsum2fyn
PubMed16924113
UniProtQ02762|UCRI_CERSP Ubiquinol-cytochrome c reductase iron-sulfur subunit (Gene Name=petA)

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