Structure of PDB 2fn0 Chain A Binding Site BS01

Receptor Information

>2fn0 Chain A (length=408) Species: 630 (Yersinia enterocolitica)

KISEFLHEEQWLPTISGVLRQFAEEECYVYERPPCWYLGKGCQARLHINA
DGTQATFIDDAGEQKWAVDSIADCARRFMAHPQVKGRRVYGQVGFNFAAH
ARGIAFNAGEWPLLTLTVPREELIFEKGNVTVYADAPLAVDTALNGEAYK
QQVARAVAEIRRGEYVKVIVSRAIPLPSRIDMPATLLYGRQANTPVRSFM
FRQEGREALGFSPELVMSVTGNKVVTEPLAGTRDRMGNPEHNKAKEAELL
HDSKEVLEHILSVKEAIAELEAVCLPGSVVVEDLMSVRQRGSVQHLGSGV
SGQLAENKDAWDAFTVLFPSITASGIPKNAALNAIMQIEKTPRELYSGAI
LLLDDTRFDAALVLRSVFQDSQRCWIQAGAGIIAQSTPERELTETREKLA
SIAPYLMV

Ligand information

• Ligand ID: ACT
• InChI: InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
• InChIKey: QTBSBXVTEAMEQO-UHFFFAOYSA-M
• SMILES:
  ACDLabs 10.04: [O-]C(=O)C
  OpenEye OEToolkits 1.5.0: CC(=O)[O-]
  CACTVS 3.341: CC([O-])=O
• Formula: C2 H3 O2
• Name: ACETATE ION
• DrugBank: DB14511
• PDB chain: 2fn0 Chain A Residue 603

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2fn0 Crystal Structures of Yersinia enterocolitica Salicylate Synthase and its Complex with the Reaction Products Salicylate and Pyruvate.
• Resolution: 1.85 Å
• Binding residue (original residue number in PDB): Y372 L390 R391 A404 G405
• Binding residue (residue number reindexed from 1): Y346 L364 R365 A378 G379
• Annotation score: 1

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

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:2fn0, PDBe:2fn0, PDBj:2fn0
• PDBsum: 2fn0
• PubMed: 16434053
• UniProt: Q9X9I8