Structure of PDB 1khz Chain B Binding Site BS01

Receptor Information

>1khz Chain B (length=202) Species: 562 (Escherichia coli)

PVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVRREIFERG
HAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIEEGESVED
VARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDATTASGIH
GLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQALKNE
WA

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 1khz Chain B Residue 301

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1khz Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase.
• Resolution: 2.04 Å
• Binding residue (original residue number in PDB): E112 E116 E164
• Binding residue (residue number reindexed from 1): E105 E109 E157
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.6.1.13: ADP-ribose diphosphatase.

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

External links

• PDB: RCSB:1khz, PDBe:1khz, PDBj:1khz
• PDBsum: 1khz
• PubMed: 12135348
• UniProt: Q93K97|ADPP_ECOLI ADP-ribose pyrophosphatase (Gene Name=nudF)