Structure of PDB 2fyn Chain R

Receptor sequence
>2fynR (length=179) Species: 1063 (Cereibacter sphaeroides) [Search protein sequence]
GTRRDFLYYATAGAGAVATGAAVWPLINQMNPSADVQALASIFVDVSSVE
PGVQLTVKFLGKPIFIRRRTEADIELGRSVQLGQLVDTNARNANIDAGAE
ATDQNRTLDEAGEWLVMWGVCTHLGCSPIGGVSGDFGGWFCPCHGSHYDS
AGRIRKGPAPENLPIPLAKFIDETTIQLG
3D structure
PDB2fyn Surface-modulated motion switch: Capture and release of iron-sulfur protein in the cytochrome bc1 complex.
ChainR
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FES R C129 H131 L132 C134 C149 C151 H152 S154 C121 H123 L124 C126 C141 C143 H144 S146
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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