Structure of PDB 1vk6 Chain A

Receptor sequence
>1vk6A (length=257) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
HMDRIIEKLDHGWWVVSHEQKLWLPKGELPYGEAANFDLVGQRALQIGEW
QGEPVWLVQQQRRHDMGSVRQVIDLDVGLFQLAGRGVQLAEFYRSHKYCG
YCGHEMYPSKTEWAMLCSHCRERYYPQIAPCIIVAIRRDDSILLAQHTRH
RNGVHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPQS
LMTAFMAEYDSGDIVIDPKELLEANWYRYDDLPLLPPPGTVARRLIEDTV
AMCRAEY
3D structure
PDB1vk6 Crystal structure of NADH pyrophosphatase (1790429) from Escherichia coli k12 at 2.20 A resolution
ChainA
Resolution2.2 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 ZN A C98 C101 C116 C119 C99 C102 C117 C120
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

View graph for
Biological Process
External links
PDB RCSB:1vk6, PDBe:1vk6, PDBj:1vk6
PDBsum1vk6
PubMed
UniProtP32664|NUDC_ECOLI NAD-capped RNA hydrolase NudC (Gene Name=nudC)

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