Structure of PDB 2bs3 Chain B

Receptor sequence
>2bs3B (length=239) Species: 844 (Wolinella succinogenes) [Search protein sequence]
MGRMLTIRVFKYDPQSAVSKPHFQEYKIEEAPSMTIFIVLNMIRETYDPD
LNFDFVCRAGICGSCGMMINGRPSLACRTLTKDFEDGVITLLPLPAFKLI
KDLSVDTGNWFNGMSQRVESWIHAQKEHDISKLEERIEPEVAQEVFELDR
CIECGCCIAACGTKIMREDFVGAAGLNRVVRFMIDPHDERTDEDYYELIG
DDDGVFGCMTLLACHDVCPKNLPLQSKIAYLRRKMVSVN
3D structure
PDB2bs3 Experimental Support for the E-Pathway Hypothesis of Coupled Transmembrane Electron and Proton Transfer in Dihemic Quinol:Fumarate Reductase
ChainB
Resolution2.19 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.3.5.1: succinate dehydrogenase.
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 B C57 R58 G60 C62 G63 C65 C77 C57 R58 G60 C62 G63 C65 C77
BS02 F3S B C161 T163 F170 C208 M209 T210 L211 L212 C214 C161 T163 F170 C208 M209 T210 L211 L212 C214
BS03 SF4 B C151 I152 E153 C154 G155 C157 C218 C151 I152 E153 C154 G155 C157 C218
Gene Ontology
Molecular Function
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051537 2 iron, 2 sulfur cluster binding
GO:0051538 3 iron, 4 sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006099 tricarboxylic acid cycle
GO:0009060 aerobic respiration
GO:0022904 respiratory electron transport chain
Cellular Component
GO:0005886 plasma membrane

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Molecular Function

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Cellular Component
External links
PDB RCSB:2bs3, PDBe:2bs3, PDBj:2bs3
PDBsum2bs3
PubMed16380425
UniProtP17596|FRDB_WOLSU Fumarate reductase iron-sulfur subunit (Gene Name=frdB)

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