Structure of PDB 2b76 Chain A

Receptor sequence
>2b76A (length=577) Species: 562 (Escherichia coli) [Search protein sequence]
MQTFQADLAIVGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAQ
GGSAAVAQDHDSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLELW
GCPWSRRPDGSVNVRRFGGMKIERTWFAADKTGFHMLHTLFQTSLQFPQI
QRFDEHFVLDILVDDGHVRGLVAMNMMEGTLVQIRANAVVMATGGAGRVY
RYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPTGLPGSGILMTEGCRG
EGGILVNKNGYRYLQDYGMGPETPLGEPKNKYMELGPRDKVSQAFWHEWR
KGNTISTPRGDVVYLDLRHLGEKKLHERLPFICELAKAYVGVDPVKEPIP
VRPTAHYTMGGIETDQNCETRIKGLFAVGECSSVGLHGANRLGSNSLAEL
VVFGRLAGEQATERAATAGNGNEAAIEAQAAGVEQRLKDLVNQDGGENWA
KIRDEMGLAMEEGCGIYRTPELMQKTIDKLAELQERFKRVRITDTSSVFN
TDLLYTIELGHGLNVAECMAHSAMARKESRGAHQRLDEGCTERDDVNFLK
HTLAFRDADGTTRLEYSDVKITTLPPA
3D structure
PDB2b76 Fumarate Reductase and Succinate Oxidase Activity of Escherichia coli Complex II Homologs Are Perturbed Differently by Mutation of the Flavin Binding Domain
ChainA
Resolution3.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A47 F116 T203 Q230 H232 L242 E245 R248 R287 H355 Y356 R390
Catalytic site (residue number reindexed from 1) A48 F117 T204 Q231 H233 L243 E246 R249 R288 H356 Y357 R391
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 FAD A G11 G14 S36 S43 H44 T45 A47 A48 Q49 G50 G51 V157 T192 G193 T203 D211 L242 Y356 G378 E379 S393 S395 L396 L399 G12 G15 S37 S44 H45 T46 A48 A49 Q50 G51 G52 V158 T193 G194 T204 D212 L243 Y357 G379 E380 S394 S396 L397 L400
Gene Ontology
Molecular Function
GO:0000104 succinate dehydrogenase activity
GO:0000166 nucleotide binding
GO:0005515 protein binding
GO:0008177 succinate dehydrogenase (quinone) activity
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0006113 fermentation
GO:0006974 DNA damage response
GO:0009061 anaerobic respiration
GO:0019645 anaerobic electron transport chain
GO:0022900 electron transport chain
GO:0044780 bacterial-type flagellum assembly
Cellular Component
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0045283 fumarate reductase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2b76, PDBe:2b76, PDBj:2b76
PDBsum2b76
PubMed16484232
UniProtP00363|FRDA_ECOLI Fumarate reductase flavoprotein subunit (Gene Name=frdA)

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