Structure of PDB 5isy Chain C Binding Site BS01
Receptor Information
>5isy Chain C (length=249) Species:
83333
(Escherichia coli K-12) [
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DRIIEKDHGWWVVSHEQKLWLPKGELPYGEAANFDLVGQRALQIGEWQGE
PVWLVQQQRRHDMGSVRQVIDLDVGLFQLAGRGVQLAEFYRSHKYCGYCG
HEMYPSKTEWAMLCSHCRERYYPQIAPCIIVAIRRDDSILLAQHTRHRNG
VHTVLAGFVEVGETLEQAVAREVMEQSGIKVKNLRYVTSQPWPFPQSLMT
AFMAEYDSGDIVIDPKELLEANWYRYDDLPLLPPPGTVARRLIEDTVAM
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
5isy Chain C Residue 301 [
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Receptor-Ligand Complex Structure
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PDB
5isy
Structural basis of prokaryotic NAD-RNA decapping by NudC
Resolution
2.354 Å
Binding residue
(original residue number in PDB)
C98 C101 C116 C119
Binding residue
(residue number reindexed from 1)
C96 C99 C114 C117
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.6.1.-
3.6.1.22
: NAD(+) diphosphatase.
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
PDBsum
5isy
PubMed
27561816
UniProt
P32664
|NUDC_ECOLI NAD-capped RNA hydrolase NudC (Gene Name=nudC)
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