Structure of PDB 5isy Chain C Binding Site BS01

Receptor Information
>5isy Chain C (length=249) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DRIIEKDHGWWVVSHEQKLWLPKGELPYGEAANFDLVGQRALQIGEWQGE
PVWLVQQQRRHDMGSVRQVIDLDVGLFQLAGRGVQLAEFYRSHKYCGYCG
HEMYPSKTEWAMLCSHCRERYYPQIAPCIIVAIRRDDSILLAQHTRHRNG
VHTVLAGFVEVGETLEQAVAREVMEQSGIKVKNLRYVTSQPWPFPQSLMT
AFMAEYDSGDIVIDPKELLEANWYRYDDLPLLPPPGTVARRLIEDTVAM
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain5isy Chain C Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5isy Structural basis of prokaryotic NAD-RNA decapping by NudC
Resolution2.354 Å
Binding residue
(original residue number in PDB)
C98 C101 C116 C119
Binding residue
(residue number reindexed from 1)
C96 C99 C114 C117
Annotation score1
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

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Molecular Function

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

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