Structure of PDB 1qor Chain A

Receptor sequence
>1qorA (length=326) Species: 562 (Escherichia coli) [Search protein sequence]
ATRIEFHKHGGPEVLQAVEFTPADPAENEIQVENKAIGINFIDTYIRSGL
YPPPSLPSGLGTEAAGIVSKVGSGVKHIKAGDRVVYAQSALGAYSSVHNI
IADKAAILPAAISFEQAAASFLKGLTVYYLLRKTYEIKPDEQFLFHAAAG
GVGLIACQWAKALGAKLIGTVGTAQKAQSALKAGAWQVINYREEDLVERL
KEITGGKKVRVVYDSVGRDTWERSLDCLQRRGLMVSFGNSSGAVTGVNLG
ILNQKGSLYVTRPSLQGYITTREELTEASNELFSLIASGVIKVDVAEQQK
YPLKDAQRAHEILESRATQGSSLLIP
3D structure
PDB1qor Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N41 F42 I43 Y46 T63 E64
Catalytic site (residue number reindexed from 1) N40 F41 I42 Y45 T62 E63
Enzyme Commision number 1.6.5.5: NADPH:quinone reductase.
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 NDP A F42 Y46 T127 Y130 G151 G152 V153 V172 G173 K177 Y192 S216 F238 S241 S242 S265 R317 F41 Y45 T126 Y129 G150 G151 V152 V171 G172 K176 Y191 S215 F237 S240 S241 S264 R316
Gene Ontology
Molecular Function
GO:0003960 NADPH:quinone reductase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0035925 mRNA 3'-UTR AU-rich region binding
GO:0042803 protein homodimerization activity
GO:0070402 NADPH binding
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:1qor, PDBe:1qor, PDBj:1qor
PDBsum1qor
PubMed7602590
UniProtP28304|QOR1_ECOLI Quinone oxidoreductase 1 (Gene Name=qorA)

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