Structure of PDB 1l0v Chain M Binding Site BS01

Receptor Information
>1l0v Chain M (length=577) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MQTFQADLAIVGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAE
GGSAAVAQDHDSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLELW
GCPWSRRPDGSVNVRRFGGMKIERTWFAADKTGFHMLHTLFQTSLQFPQI
QRFDEHFVLDILVDDGHVRGLVAMNMMEGTLVQIRANAVVMATGGAGRVY
RYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPTGLPGSGILMTEGCRG
EGGILVNKNGYRYLQDYGMGPETPLGEPKNKYMELGPRDKVSQAFWHEWR
KGNTISTPRGDVVYLDLRHLGEKKLHERLPFICELAKAYVGVDPVKEPIP
VRPTAHYTMGGIETDQNCETRIKGLFAVGECSSVGLHGANRLGSNSLAEL
VVFGRLAGEQATERAATAGNGNEAAIEAQAAGVEQRLKDLVNQDGGENWA
KIRDEMGLAMEEGCGIYRTPELMQKTIDKLAELQERFKRVRITDTSSVFN
TDLLYTIELGHGLNVAECMAHSAMARKESRGAHQRLDEGCTERDDVNFLK
HTLAFRDADGTTRLEYSDVKITTLPPA
Ligand information
Ligand IDOAA
InChIInChI=1S/C4H4O5/c5-2(4(8)9)1-3(6)7/h1H2,(H,6,7)(H,8,9)/p-1
InChIKeyKHPXUQMNIQBQEV-UHFFFAOYSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04[O-]C(=O)CC(=O)C(=O)O
OpenEye OEToolkits 1.5.0C(C(=O)C(=O)O)C(=O)[O-]
CACTVS 3.341OC(=O)C(=O)CC([O-])=O
FormulaC4 H3 O5
NameOXALOACETATE ION
ChEMBL
DrugBankDB02637
ZINC
PDB chain1l0v Chain M Residue 802 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1l0v Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site.
Resolution3.3 Å
Binding residue
(original residue number in PDB)		F116 H232 T244 E245 R287 H355 R390
Binding residue
(residue number reindexed from 1)		F117 H233 T245 E246 R288 H356 R391
Annotation score2
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.
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
PDBsum1l0v
PubMed11850430
UniProtP00363|FRDA_ECOLI Fumarate reductase flavoprotein subunit (Gene Name=frdA)

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