Structure of PDB 2fn1 Chain A

Receptor sequence

>2fn1A (length=408) Species: 630 (Yersinia enterocolitica)

KISEFLHEEQWLPTISGVLRQFAEEECYVYERPPCWYLGKGCQARLHINA
DGTQATFIDDAGEQKWAVDSIADCARRFMAHPQVKGRRVYGQVGFNFAAH
ARGIAFNAGEWPLLTLTVPREELIFEKGNVTVYADAPLAVDTALNGEAYK
QQVARAVAEIRRGEYVKVIVSRAIPLPSRIDMPATLLYGRQANTPVRSFM
FRQEGREALGFSPELVMSVTGNKVVTEPLAGTRDRMGNPEHNKAKEAELL
HDSKEVLEHILSVKEAIAELEAVCLPGSVVVEDLMSVRQRGSVQHLGSGV
SGQLAENKDAWDAFTVLFPSITASGIPKNAALNAIMQIEKTPRELYSGAI
LLLDDTRFDAALVLRSVFQDSQRCWIQAGAGIIAQSTPERELTETREKLA
SIAPYLMV

3D structure

• PDB: 2fn1 Crystal Structures of Yersinia enterocolitica Salicylate Synthase and its Complex with the Reaction Products Salicylate and Pyruvate.
• Chain: A
• Resolution: 2.1 Å

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

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	E284 E420	E258 E394
BS02	PYR	A	Y372 L390 R391 A404 G405 K424	Y346 L364 R365 A378 G379 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

External links

• PDB: RCSB:2fn1, PDBe:2fn1, PDBj:2fn1
• PDBsum: 2fn1
• PubMed: 16434053
• UniProt: Q9X9I8