Structure of PDB 5kdr Chain B Binding Site BS02

Receptor Information

>5kdr Chain B (length=250) Species: 273036 (Staphylococcus aureus RF122)

IMTKCPKCKKIMYTKELAENLNVCFNCDHHIALTAYKRIEAISDEGSFTE
FDKGMTSANPLDFPSYLEKIEKDQQKTGLKEAVVTGTAQLDGMKFGVAVM
DSRFRMGSMGSVIGEKICRIIDYCTENRLPFILFSASGGARMQEGIISLM
QMGKTSVSLKRHSDAGLLYISYLTHPTTGGVSASFASVGDINLSEPKALI
GFAGRRVIEQTINDFQTAEFLLEHGQLDKVVHRNDMRQTLSEILKIHQEV

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 5kdr Chain B Residue 304

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5kdr Crystal Structure of Carboxyltransferase from Staphylococcus aureus Bound to the Antibacterial Agent Moiramide B.
• Resolution: 2.6 Å
• Binding residue (original residue number in PDB): C33 C36 C52 C55
• Binding residue (residue number reindexed from 1): C5 C8 C24 C27
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): G207 G208
• Catalytic site (residue number reindexed from 1): G179 G180
• Enzyme Commision number: 2.1.3.15: acetyl-CoA carboxytransferase.

Gene Ontology

Molecular Function

• GO:0003989 acetyl-CoA carboxylase activity
• GO:0005524 ATP binding
• GO:0008270 zinc ion binding
• GO:0016740 transferase activity
• GO:0016743 carboxyl- or carbamoyltransferase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006633 fatty acid biosynthetic process
• GO:2001295 malonyl-CoA biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0009317 acetyl-CoA carboxylase complex

External links

• PDB: RCSB:5kdr, PDBe:5kdr, PDBj:5kdr
• PDBsum: 5kdr
• PubMed: 27471863
• UniProt: Q2FXM6|ACCD_STAA8 Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (Gene Name=accD)