Structure of PDB 1kf6 Chain A

Receptor sequence

>1kf6A (length=577) Species: 562 (Escherichia coli) [Search protein sequence]

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

3D structure

PDB

1kf6 Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site.

Chain

Resolution

2.7 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	OAA	A	F116 H232 T244 H355 R390	F117 H233 T245 H356 R391
BS02	FAD	A	G11 A15 S36 K37 S43 H44 T45 A48 G50 G51 V157 A191 T192 T203 D211 H355 Y356 E379 R390 S393 S395 L396 L399	G12 A16 S37 K38 S44 H45 T46 A49 G51 G52 V158 A192 T193 T204 D212 H356 Y357 E380 R391 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

View graph for
Molecular Function

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Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:1kf6, PDBe:1kf6, PDBj:1kf6
PDBsum	1kf6
PubMed	11850430
UniProt	P00363\|FRDA_ECOLI Fumarate reductase flavoprotein subunit (Gene Name=frdA)

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