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Structure of PDB 2fn0 Chain B

Receptor sequence
>2fn0B (length=412) Species: 630 (Yersinia enterocolitica) [Search protein sequence]
MKISEFLHLALPEEQWLPTISGVLRQFAEEECYVYERPPCWYLGKGCQAR
LHINADGTQATFIDDAGEQKWAVDSIADCARRFMAHPQVKGRRVYGQVGF
NFAAHARGIAFNAGEWPLLTLTVPREELIFEKGNVTVYADPLAVDTALNG
EAYKQQVARAVAEIRRGEYVKVIVSRAIPLPSRIDMPATLLYGRQANTPV
RSFMFRQEGREALGFSPELVMSVTGNKVVTEPLAGTRDRMGNPEHNKAKE
AELLHDSKEVLEHILSVKEAIAELEAVCLPGSVVVEDLMSVRQRGSVQHL
GSGVSGQLAENKDAWDAFTVLFPSITASGIPKNAALNAIMQIEKTPRELY
SGAILLLDDTRFDAALVLRSVFQDSQRCWIQAGAGIIAQSTPERELTETR
EKLASIAPYLMV
3D structure
PDB2fn0 Crystal Structures of Yersinia enterocolitica Salicylate Synthase and its Complex with the Reaction Products Salicylate and Pyruvate.
ChainB
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) K171 E218 A234 E262 H299 T326 Y350 R369 G385 E398 K402
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 E262 E398
BS02 PO4 B A256 G257 T258 E284 A406 G407 E420 K424 A234 G235 T236 E262 A384 G385 E398 K402
BS03 ACT B Y372 L390 R391 A404 G405 K424 Y350 L368 R369 A382 G383 K402
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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External links

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