Structure of PDB 3s23 Chain A

Receptor sequence
>3s23A (length=334) Species: 340 (Xanthomonas campestris pv. campestris) [Search protein sequence]
LVPRGSHMLFQNVSIAGLAHIDAPHTLTSKEINERLQPTYDRLGIKTDVL
GDVAGIHARRLWDQDVQASDAATQAARKALIDANIGIEKIGLLINTSVSR
DYLEPSTASIVSGNLGVSDHCMTFDVANACLAFINGMDIAARMLERGEID
YALVVDGETANLVYEKTLERMTSPDVTEEEFRNELAALTLGCGAAAMVMA
RSELVPDAPRYKGGVTRSATEWNKLTRLLLIEGIKLAQKTFVAAKQVLGW
AVEELDQFVIHQVSRPHTAAFVKSFGIDPAKVMTIFGEHGNIGPASVPIV
LSKLKELGRLKKGDRIALLGIGSGLNCSMAEVVW
3D structure
PDB3s23 Crystal Structures of Xanthomonas campestris OleA Reveal Features That Promote Head-to-Head Condensation of Two Long-Chain Fatty Acids.
ChainA
Resolution1.9484 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.3.20: acyl-CoA:acyl-CoA alkyltransferase.
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 MN A H38 D76 H25 D63
BS02 MN A K336 W358 K312 W334
BS03 CER A A142 C143 L253 L254 H285 V287 H291 I345 G346 S347 A129 C130 L229 L230 H261 V263 H267 I321 G322 S323
BS04 XE A F265 F282 F299 F241 F258 F275
BS05 XE A I28 A29 G30 P222 I15 A16 G17 P209
Gene Ontology
Molecular Function
GO:0004315 3-oxoacyl-[acyl-carrier-protein] synthase activity
GO:0016746 acyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0044550 secondary metabolite biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:3s23, PDBe:3s23, PDBj:3s23
PDBsum3s23
PubMed22524624
UniProtQ8PDX2|OLEA_XANCP Acyl-CoA:acyl-CoA alkyltransferase (Gene Name=oleA)

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