Structure of PDB 2fn0 Chain A

Receptor sequence
>2fn0A (length=408) Species: 630 (Yersinia enterocolitica) [Search protein sequence]
KISEFLHEEQWLPTISGVLRQFAEEECYVYERPPCWYLGKGCQARLHINA
DGTQATFIDDAGEQKWAVDSIADCARRFMAHPQVKGRRVYGQVGFNFAAH
ARGIAFNAGEWPLLTLTVPREELIFEKGNVTVYADAPLAVDTALNGEAYK
QQVARAVAEIRRGEYVKVIVSRAIPLPSRIDMPATLLYGRQANTPVRSFM
FRQEGREALGFSPELVMSVTGNKVVTEPLAGTRDRMGNPEHNKAKEAELL
HDSKEVLEHILSVKEAIAELEAVCLPGSVVVEDLMSVRQRGSVQHLGSGV
SGQLAENKDAWDAFTVLFPSITASGIPKNAALNAIMQIEKTPRELYSGAI
LLLDDTRFDAALVLRSVFQDSQRCWIQAGAGIIAQSTPERELTETREKLA
SIAPYLMV
3D structure
PDB2fn0 Crystal Structures of Yersinia enterocolitica Salicylate Synthase and its Complex with the Reaction Products Salicylate and Pyruvate.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K193 E240 A256 E284 H321 T348 Y372 R391 G407 E420 K424
Catalytic site (residue number reindexed from 1) K167 E214 A230 E258 H295 T322 Y346 R365 G381 E394 K398
Enzyme Commision number ?
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 ACT A Y372 L390 R391 A404 G405 Y346 L364 R365 A378 G379
BS02 MG A E284 E420 E258 E394
BS03 PO4 A A256 G257 T258 E284 G407 E420 K424 A230 G231 T232 E258 G381 E394 K398
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008909 isochorismate synthase activity
GO:0016833 oxo-acid-lyase activity
GO:0016835 carbon-oxygen lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0009058 biosynthetic process
GO:0019290 siderophore biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2fn0, PDBe:2fn0, PDBj:2fn0
PDBsum2fn0
PubMed16434053
UniProtQ9X9I8

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