Structure of PDB 1y4z Chain C

Receptor sequence
>1y4zC (length=217) Species: 562 (Escherichia coli) [Search protein sequence]
MQFLNMFFFDIYPYIAGAVFLIGSWLRYDYGQYTWRAASSQMLDRKGMNL
ASNLFHIGILGIFVGHFFGMLTLPIEVKQKMAMFAGGASGVLCLIGGVLL
LKRRLFSPRVRATTTGADILILSLLVIQCALGLLTIPFSAQHMDGSEMMK
LVGWAQSVVTFHGGASQHLDGVAFIFRLHLVLGMTLFLLFPFSRLIHIWS
VPVEYLTRKYQLVRARH
3D structure
PDB1y4z Structural and Biochemical Characterization of a Quinol Binding Site of Escherichia coli Nitrate Reductase A
ChainC
Resolution2.0 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 I59 I62 H66 M70 A90 Q136 C137 G140 I144 M156 L159 H187 L188 G191 F195 I59 I62 H66 M70 A82 Q128 C129 G132 I136 M148 L151 H179 L180 G183 F187
BS03 PCI C G65 H66 G69 K86 A90 M156 G65 H66 G69 K78 A82 M148 MOAD: Ki=57nM
PDBbind-CN: -logKd/Ki=7.24,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:1y4z, PDBe:1y4z, PDBj:1y4z
PDBsum1y4z
PubMed15615728
UniProtP11350|NARI_ECOLI Respiratory nitrate reductase 1 gamma chain (Gene Name=narI)

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