Structure of PDB 1l0v Chain M

Receptor sequence

>1l0vM (length=577) Species: 562 (Escherichia coli) [Search protein sequence]

MQTFQADLAIVGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAE
GGSAAVAQDHDSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLELW
GCPWSRRPDGSVNVRRFGGMKIERTWFAADKTGFHMLHTLFQTSLQFPQI
QRFDEHFVLDILVDDGHVRGLVAMNMMEGTLVQIRANAVVMATGGAGRVY
RYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPTGLPGSGILMTEGCRG
EGGILVNKNGYRYLQDYGMGPETPLGEPKNKYMELGPRDKVSQAFWHEWR
KGNTISTPRGDVVYLDLRHLGEKKLHERLPFICELAKAYVGVDPVKEPIP
VRPTAHYTMGGIETDQNCETRIKGLFAVGECSSVGLHGANRLGSNSLAEL
VVFGRLAGEQATERAATAGNGNEAAIEAQAAGVEQRLKDLVNQDGGENWA
KIRDEMGLAMEEGCGIYRTPELMQKTIDKLAELQERFKRVRITDTSSVFN
TDLLYTIELGHGLNVAECMAHSAMARKESRGAHQRLDEGCTERDDVNFLK
HTLAFRDADGTTRLEYSDVKITTLPPA

3D structure

PDB

1l0v Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site.

Chain

Resolution

3.3 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	F116 H232 R287 H355 Y356 R390
Catalytic site (residue number reindexed from 1)	F117 H233 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	OAA	M	F116 H232 T244 E245 R287 H355 R390	F117 H233 T245 E246 R288 H356 R391
BS02	FAD	M	G13 G14 K37 H44 T45 A48 E49 G50 G51 F156 V157 T192 N204 D211 H355 Y356 E379 S393 S395 L396 L399	G14 G15 K38 H45 T46 A49 E50 G51 G52 F157 V158 T193 N205 D212 H356 Y357 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:1l0v, PDBe:1l0v, PDBj:1l0v
PDBsum	1l0v
PubMed	11850430
UniProt	P00363\|FRDA_ECOLI Fumarate reductase flavoprotein subunit (Gene Name=frdA)

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