Structure of PDB 3u0o Chain A Binding Site BS01

Receptor Information

>3u0o Chain A (length=319) Species: 83333 (Escherichia coli K-12)

ILHSEQAKFVDPNLLVGNETRDDAAVYDLGNGTSVISTTDFFMPIVDNPF
DFGRIAATNAISDIFAMGGKPIMAIAILGWPINKLSPEIAREVTEGGRYA
CRQAGIALAGGHSIDAPEPIFGLAVTGIVPTERVKKNSTAQAGCKLFLTK
PLGIGVLTTAEKKSLLKPEHQGLATEVMCRMNIAGASFANIEGVKAMTDV
TGFGLLGHLSEMCQGAGVQARVDYEAIPKLPGVEEYIKLGAVPGGTERNF
ASYGHLMGEMPREVRDLLCDPQTSGGLLLAVMPEAENEVKATAAEFGIEL
TAIGELVPARGGRAMVEIR

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: 3u0o Chain A Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3u0o Structural insights into the catalytic mechanism of Escherichia coli selenophosphate synthetase.
• Resolution: 2.25 Å
• Binding residue (original residue number in PDB): D51 D91 D227
• Binding residue (residue number reindexed from 1): D23 D63 D199
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.7.9.3: selenide, water dikinase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004756 selenide, water dikinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0042802 identical protein binding
• GO:0042803 protein homodimerization activity
• GO:0046872 metal ion binding

Biological Process

• GO:0016260 selenocysteine biosynthetic process
• GO:0016310 phosphorylation
• GO:0070329 tRNA seleno-modification

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:3u0o, PDBe:3u0o, PDBj:3u0o
• PDBsum: 3u0o
• PubMed: 22081394
• UniProt: P16456|SELD_ECOLI Selenide, water dikinase (Gene Name=selD)