Structure of PDB 3fj4 Chain A

Receptor sequence
>3fj4A (length=371) Species: 220664 (Pseudomonas protegens Pf-5) [Search protein sequence]
HASAIESIETIIVDLPTIRPHKLAMHTMQNQTLVLIRLRCADGIEGLGES
TTIGGLAYGNESPDSIKTNIDRFVAPLLIGQDASNINAAMLRLEQSIRGN
TFAKSGIESALLDAQGKRLGLPVSELLGGRVRDALPVAWTLASGDTAKDI
AEAQKMLDLRRHRIFKLKIGAGEVDRDLAHVIAIKKALGDSASVRVDVNQ
AWDEAVALRACRILGGNGIDLIEQPISRNNRAGMVRLNASSPAPIMADES
IECVEDAFNLAREGAASVFALKIAKNGGPRATLRTAAIAEAAGIGLYGGT
MLEGGIGTLASAHAFLTLNKLSWDTELFGPLLLTEDILAEPPVYRDFHLH
VSKAPGLGLSLDEERLAFFRR
3D structure
PDB3fj4 Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H24 T55 G58 T143 K169 K171 D200 N202 E226 D251 E252 S253 I254 K275 Y300 G302 T303 M304 H316 T328 E329 L330
Catalytic site (residue number reindexed from 1) H21 T52 G55 T140 K166 K168 D197 N199 E223 D248 E249 S250 I251 K272 Y297 G299 T300 M301 H313 T325 E326 L327
Enzyme Commision number 5.5.1.1: muconate cycloisomerase.
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 MUC A I56 Y61 T143 K169 K171 D200 K275 T303 E329 I53 Y58 T140 K166 K168 D197 K272 T300 E326
BS02 MG A D200 E226 D251 D197 E223 D248
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0018849 muconate cycloisomerase activity
GO:0018850 chloromuconate cycloisomerase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process
GO:0009063 amino acid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3fj4, PDBe:3fj4, PDBj:3fj4
PDBsum3fj4
PubMed19220063
UniProtQ4K9X1

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