Structure of PDB 2qv7 Chain A Binding Site BS01

Receptor Information

>2qv7 Chain A (length=303) Species: 282458 (Staphylococcus aureus subsp. aureus MRSA252)

GSHMMRKRARIIYNPTSGKEQFKRELPDALIKLEKAGYETSAYATEKIGD
ATLEAERAMHENYDVLIAAGGDGTLNEVVNGIAEKPNRPKLGVIPMGTVN
DFGRALHIPNDIMGALDVIIEGHSTKVDIGKMNNRYFINLAAGGQLTQGP
FAYYIKGFEMLPQMKAVDLRIEYDGNVFQGEALLFFLGLTNSMAGFEKLV
PDAKLDDGYFTLIIVEKSNLAELGHIMTLASRGEHTKHPKVIYEKAKAIN
ISSFTDLQLNVDGEYGGKLPANFLNLERHIDVFAPNDIVNEELINNDHVD
DNL

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: 2qv7 Chain A Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2qv7 Analysis of the Staphylococcus aureus DgkB Structure Reveals a Common Catalytic Mechanism for the Soluble Diacylglycerol Kinases.
• Resolution: 2.3 Å
• Binding residue (original residue number in PDB): K213 D216 Y218
• Binding residue (residue number reindexed from 1): K204 D207 Y209
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.7.1.107: diacylglycerol kinase (ATP).

Gene Ontology

Molecular Function

• GO:0004143 ATP-dependent diacylglycerol kinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0008654 phospholipid biosynthetic process
• GO:0016310 phosphorylation

Cellular Component

• GO:0005886 plasma membrane

External links

• PDB: RCSB:2qv7, PDBe:2qv7, PDBj:2qv7
• PDBsum: 2qv7
• PubMed: 18611377
• UniProt: Q6GFF9|DAGK_STAAR Diacylglycerol kinase (Gene Name=dagK)