Structure of PDB 1y5n Chain C

Receptor sequence
>1y5nC (length=217) Species: 562 (Escherichia coli) [Search protein sequence]
MQFLNMFFFDIYPYIAGAVFLIGSWLRYDYGQYTWRAASSQMLDRKGMNL
ASNLFHIGILGIFVGHFFGMLTLPIEVAQKMAMFAGGASGVLCLIGGVLL
LKRRLFSPRVRATTTGADILILSLLVIQCALGLLTIPFSAQHMDGSEMMK
LVGWAQSVVTFHGGASQHLDGVAFIFRLHLVLGMTLFLLFPFSRLIHIWS
VPVEYLTRKYQLVRARH
3D structure
PDB1y5n Structural and Biochemical Characterization of a Quinol Binding Site of Escherichia coli Nitrate Reductase A
ChainC
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.7.5.1: nitrate reductase (quinone).
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 HEM C S39 S40 Q41 M48 F55 H56 R112 R202 H205 I206 S39 S40 Q41 M48 F55 H56 R104 R194 H197 I198
BS02 HEM C I62 H66 A90 Q136 C137 G140 M156 L159 H187 L188 G191 M192 F195 I62 H66 A82 Q128 C129 G132 M148 L151 H179 L180 G183 M184 F187
BS03 PCI C G65 H66 G69 A90 M156 G65 H66 G69 A82 M148 MOAD: Ki=57nM
Gene Ontology
Molecular Function
GO:0008940 nitrate reductase activity
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0160182 nitrate reductase (quinone) activity
Biological Process
GO:0009061 anaerobic respiration
GO:0019645 anaerobic electron transport chain
GO:0042126 nitrate metabolic process
GO:0042128 nitrate assimilation
Cellular Component
GO:0005886 plasma membrane
GO:0009325 nitrate reductase complex
GO:0016020 membrane
GO:0044799 NarGHI complex

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Cellular Component
External links
PDB RCSB:1y5n, PDBe:1y5n, PDBj:1y5n
PDBsum1y5n
PubMed15615728
UniProtP11350|NARI_ECOLI Respiratory nitrate reductase 1 gamma chain (Gene Name=narI)

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