Structure of PDB 1oxh Chain D Binding Site BS01

Receptor Information
>1oxh Chain D (length=408) Species: 1313 (Streptococcus pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KLNRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNA
AEIQDFPFDKYFVKKDTNRFDNYSLYALYAAQEAVNHANLDVEALNRDRF
GVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRF
GANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIA
GFQALTALSTTEDPTRASIPFDKDRNGFVMGEGSGMLVLESLEHAEKRGA
TILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVN
AHGTSTPANEKGESGAIVAVLGKEVPVSSTKSFTGHLLGAAGAVEAIVTI
EAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKEIPYAISNTFGFGGHNA
VLAFKRWE
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1oxh Chain D Residue 904 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1oxh The 1.3-Angstrom-Resolution Crystal Structure of beta-Ketoacyl-Acyl Carrier Protein Synthase II from Streptococcus pneumoniae.
Resolution2.09 Å
Binding residue
(original residue number in PDB)		N301 A302 E346 S391 N392
Binding residue
(residue number reindexed from 1)		N300 A301 E345 S390 N391
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) C164 H303 E314 K332 H337 F394 F396
Catalytic site (residue number reindexed from 1) C163 H302 E313 K331 H336 F393 F395
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1oxh, PDBe:1oxh, PDBj:1oxh
PDBsum1oxh
PubMed12837788
UniProtQ9FBC2

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