Structure of PDB 3cir Chain M

Receptor sequence
>3cirM (length=504) Species: 562 (Escherichia coli) [Search protein sequence]
MQTFQADLAIVGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAE
GGSAAVAQDHDSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLELW
GCPWSRRPDGSVNVRRFGGMKIERTWFAADKTGFHMLHTLFQTSLQFPQI
QRFDEHFVLDILVDDGHVRGLVAMNMMEGTLVQIRANAVVMATGGAGRVY
RYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPAGLPGSGILMTEGCRD
KVSQAFWHEWRKGNTISKKLHEFICELAKAYPVRPTAHYTMGGIETDQNC
ETRIKGLFAVGECSSVGLHGANRLGSNSLAELVVFGRLAGEQATERAATA
GNGNEAAIEAQAAGVEQRLKDLVNQDGGENWAKIRDEMGLAMEEGCGIYR
TPELMQKTIDKLAELQERFKRVRITDTSSVFNTDLLYTIELGHGLNVAEC
MAHSAMARKESRGAHQRLDEGCTERDDVNFLKHTLAFRDADGTTRLEYSD
VKIT
3D structure
PDB3cir A threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex II.
ChainM
Resolution3.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F116 H232 R287 H355 Y356 R390
Catalytic site (residue number reindexed from 1) F117 H233 R249 H288 Y289 R323
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 M G11 A12 G13 S36 K37 S43 H44 T45 A47 A48 E49 G51 H155 F156 V157 A191 T192 G193 T203 D211 H355 R390 S393 N394 S395 L396 L399 G12 A13 G14 S37 K38 S44 H45 T46 A48 A49 E50 G52 H156 F157 V158 A192 T193 G194 T204 D212 H288 R323 S326 N327 S328 L329 L332
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:3cir, PDBe:3cir, PDBj:3cir
PDBsum3cir
PubMed18385138
UniProtP00363|FRDA_ECOLI Fumarate reductase flavoprotein subunit (Gene Name=frdA)

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