Structure of PDB 1oxh Chain A

Receptor sequence
>1oxhA (length=408) Species: 1313 (Streptococcus pneumoniae) [Search protein sequence]
KLNRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNA
AEIQDFPFDKYFVKKDTNRFDNYSLYALYAAQEAVNHANLDVEALNRDRF
GVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRF
GANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIA
GFQALTALSTTEDPTRASIPFDKDRNGFVMGEGSGMLVLESLEHAEKRGA
TILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVN
AHGTSTPANEKGESGAIVAVLGKEVPVSSTKSFTGHLLGAAGAVEAIVTI
EAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKEIPYAISNTFGFGGHNA
VLAFKRWE
3D structure
PDB1oxh The 1.3-Angstrom-Resolution Crystal Structure of beta-Ketoacyl-Acyl Carrier Protein Synthase II from Streptococcus pneumoniae.
ChainA
Resolution2.09 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG A N301 A302 E346 N392 N300 A301 E345 N391
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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