Structure of PDB 1g9q Chain A

Receptor sequence
>1g9qA (length=205) Species: 562 (Escherichia coli) [Search protein sequence]
MLKPDNLPVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVR
REIFERGHAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIE
EGESVEDVARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDA
TTASLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQAL
KNEWA
3D structure
PDB1g9q The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family.
ChainA
Resolution2.3 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 APR A F28 F29 R79 A96 M98 E139 F28 F29 R79 A96 M98 E139
BS02 APR A R51 E52 S133 G135 R51 E52 S133 G135
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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Molecular Function
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Cellular Component
External links
PDB RCSB:1g9q, PDBe:1g9q, PDBj:1g9q
PDBsum1g9q
PubMed11323725
UniProtQ93K97|ADPP_ECOLI ADP-ribose pyrophosphatase (Gene Name=nudF)

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