Structure of PDB 7e44 Chain E

Receptor sequence
>7e44E (length=257) Species: 469008 (Escherichia coli BL21(DE3)) [Search protein sequence]
HMDRIIEKLDHGWWVVSHEQKLWLPKGELPYGEAANFDLVGQRALQIGEW
QGEPVWLVQQQRRHDMGSVRQVIDLDVGLFQLAGRGVQLAEFYRSHKYCG
YCGHEMYPSKTEWAMLCSHCRERYYPQIAPCIIVAIRRDDSILLAQHTRH
RNGVHTVLAGFVEVGETLEQAVAREVMEQSGIKVKNLRYVTSQPWPFPQS
LMTAFMAEYDSGDIVIDPKELLEANWYRYDDLPLLPPPGTVARRLIEDTV
AMCRAEY
3D structure
PDB7e44 Structural insights into dpCoA-RNA decapping by NudC.
ChainE
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.1.-
3.6.1.22: NAD(+) diphosphatase.
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 COD E H146 H149 T155 F160 W194 P235 A241 H147 H150 T156 F161 W195 P236 A242
BS02 ZN E C98 C101 C116 C119 C99 C102 C117 C120
BS03 COD E E111 Y124 E112 Y125
Gene Ontology
Molecular Function
GO:0000210 NAD+ diphosphatase activity
GO:0000287 magnesium ion binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0030145 manganese ion binding
GO:0035529 NADH pyrophosphatase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0110153 RNA NAD-cap (NMN-forming) hydrolase activity
Biological Process
GO:0006402 mRNA catabolic process
GO:0006734 NADH metabolic process
GO:0006742 NADP catabolic process
GO:0019677 NAD catabolic process
GO:0048255 mRNA stabilization
GO:0110155 NAD-cap decapping

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Molecular Function
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Biological Process
External links
PDB RCSB:7e44, PDBe:7e44, PDBj:7e44
PDBsum7e44
PubMed34074215
UniProtP32664|NUDC_ECOLI NAD-capped RNA hydrolase NudC (Gene Name=nudC)

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