Structure of PDB 5isy Chain C

Receptor sequence
>5isyC (length=249) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
DRIIEKDHGWWVVSHEQKLWLPKGELPYGEAANFDLVGQRALQIGEWQGE
PVWLVQQQRRHDMGSVRQVIDLDVGLFQLAGRGVQLAEFYRSHKYCGYCG
HEMYPSKTEWAMLCSHCRERYYPQIAPCIIVAIRRDDSILLAQHTRHRNG
VHTVLAGFVEVGETLEQAVAREVMEQSGIKVKNLRYVTSQPWPFPQSLMT
AFMAEYDSGDIVIDPKELLEANWYRYDDLPLLPPPGTVARRLIEDTVAM
3D structure
PDB5isy Structural basis of prokaryotic NAD-RNA decapping by NudC
ChainC
Resolution2.354 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 ZN C C98 C101 C116 C119 C96 C99 C114 C117
BS02 NAD C F160 W194 M201 V240 A241 F158 W192 M199 V238 A239
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5isy, PDBe:5isy, PDBj:5isy
PDBsum5isy
PubMed27561816
UniProtP32664|NUDC_ECOLI NAD-capped RNA hydrolase NudC (Gene Name=nudC)

[Back to BioLiP]