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Structure of PDB 2fn1 Chain B

Receptor sequence
>2fn1B (length=411) Species: 630 (Yersinia enterocolitica) [Search protein sequence]
KISEFLHLALPEEQWLPTISGVLRQFAEEECYVYERPPCWYLGKGCQARL
HINADGTQATFIDDAGEQKWAVDSIADCARRFMAHPQVKGRRVYGQVGFN
FAAHARGIAFNAGEWPLLTLTVPREELIFEKGNVTVYADPLAVDTALNGE
AYKQQVARAVAEIRRGEYVKVIVSRAIPLPSRIDMPATLLYGRQANTPVR
SFMFRQEGREALGFSPELVMSVTGNKVVTEPLAGTRDRMGNPEHNKAKEA
ELLHDSKEVLEHILSVKEAIAELEAVCLPGSVVVEDLMSVRQRGSVQHLG
SGVSGQLAENKDAWDAFTVLFPSITASGIPKNAALNAIMQIEKTPRELYS
GAILLLDDTRFDAALVLRSVFQDSQRCWIQAGAGIIAQSTPERELTETRE
KLASIAPYLMV
3D structure
PDB2fn1 Crystal Structures of Yersinia enterocolitica Salicylate Synthase and its Complex with the Reaction Products Salicylate and Pyruvate.
ChainB
Resolution2.1 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) K170 E217 A233 E261 H298 T325 Y349 R368 G384 E397 K401
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 MG B E284 E420 E261 E397
BS02 PYR B Y372 L390 R391 A404 G405 K424 Y349 L367 R368 A381 G382 K401
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
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