Structure of PDB 1khz Chain B

Receptor sequence
>1khzB (length=202) Species: 562 (Escherichia coli) [Search protein sequence]
PVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVRREIFERG
HAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIEEGESVED
VARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDATTASGIH
GLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQALKNE
WA
3D structure
PDB1khz Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase.
ChainB
Resolution2.04 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.1.13: ADP-ribose 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 MG B E112 E116 E164 E105 E109 E157
BS02 MG B A96 E116 A89 E109
BS03 ADV B F28 F29 R56 R79 A96 G97 E112 E139 E162 E164 F21 F22 R49 R72 A89 G90 E105 E132 E155 E157
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005515 protein binding
GO:0016462 pyrophosphatase activity
GO:0016787 hydrolase activity
GO:0016818 hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
GO:0019144 ADP-sugar diphosphatase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0047631 ADP-ribose diphosphatase activity
Biological Process
GO:0006753 nucleoside phosphate metabolic process
GO:0009408 response to heat
GO:0019693 ribose phosphate metabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1khz, PDBe:1khz, PDBj:1khz
PDBsum1khz
PubMed12135348
UniProtQ93K97|ADPP_ECOLI ADP-ribose pyrophosphatase (Gene Name=nudF)

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