Structure of PDB 1ox0 Chain A Binding Site BS01

Receptor Information

>1ox0 Chain A (length=414) Species: 1313 (Streptococcus pneumoniae)

PRGSHMKLNRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSD
FDVHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALYAAQEAVNHANLDVEA
LNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASG
NVAMRFGANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASI
TPFAIAGFQALTALSTTEDPTRASIPFDKDRNGFVMGEGSGMLVLESLEH
AEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPE
QVAYVNAHGTSTPANEKGESGAIVAVLGKEVPVSSTKSFTGHLLGAAGAV
EAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKEIPYAISNTFG
FGGHNAVLAFKRWE

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: 1ox0 Chain A Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1ox0 The 1.3-Angstrom-Resolution Crystal Structure of beta-Ketoacyl-Acyl Carrier Protein Synthase II from Streptococcus pneumoniae.
• Resolution: 1.3 Å
• Binding residue (original residue number in PDB): N301 A302 E346 N392
• Binding residue (residue number reindexed from 1): N306 A307 E351 N397
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): C164 H303 E314 K332 H337 F394 F396
• Catalytic site (residue number reindexed from 1): C169 H308 E319 K337 H342 F399 F401
• Enzyme Commision number: 2.3.1.179: beta-ketoacyl-[acyl-carrier-protein] synthase II.

Gene Ontology

Molecular Function

• GO:0004315 3-oxoacyl-[acyl-carrier-protein] synthase activity
• GO:0016746 acyltransferase activity
• GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
• GO:0046872 metal ion binding

Biological Process

• GO:0006633 fatty acid biosynthetic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1ox0, PDBe:1ox0, PDBj:1ox0
• PDBsum: 1ox0
• PubMed: 12837788
• UniProt: Q9FBC2