Structure of PDB 3unv Chain A

Receptor sequence
>3unvA (length=514) Species: 549 (Pantoea agglomerans) [Search protein sequence]
SFHISSGKDISLEEIARAARDHQPVTLHDEVVNRVTRSRSILESMVSDER
VIYGVNTSMGGFVNYIVPIAKASELQNNLINAVATNVGKYFDDTTVRATM
LARIVSLSRGNSAISIVNFKKLIEIYNQGIVPCIPEKGSLGGDLGPLAAI
ALVCTGQWKARYQGEQMSGAMALEKAGISPMELSFKEGLALINGTSAMVG
LGVLLYDEVKRLFDTYLTVTSLSIEGLHGKTKPFEPAVHRMKPHQGQLEV
ATTIWETLADSSLAVNEHEVEKLIAEEMDGLVKASNHQIEDAYSIRCTPQ
ILGPVADTLKNIKQTLTNELNSSNDNPLIDQTTEEVFHNGHFHGQYVSMA
MDHLNIALVTMMNLANRRIDRFMDKSNSNGLPPFLCAENAGLRLGLMGGQ
FMTASITAESRASCMPMSIQSLSTTGDFQDIVSFGLVAARRVREQLKNLK
YVFSFELLCACQAVDIRGTAGLSKRTRALYDKTRTLVPYLEEDKTISDYI
ESIAQTVLTKNSDI
3D structure
PDB3unv Insights into the mechanistic pathway of the Pantoea agglomerans phenylalanine aminomutase.
ChainA
Resolution1.54 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y78 G85 V108 L218 D318 S321 G367 D454
Catalytic site (residue number reindexed from 1) Y53 G60 V83 L191 D291 S294 G340 D427
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 SFE A Y78 G85 X168 N220 N353 F369 Y53 G60 X142 N193 N326 F342
BS02 PHE A Y78 G85 X168 L171 N353 F369 Y53 G60 X142 L144 N326 F342
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016841 ammonia-lyase activity
Biological Process
GO:0044550 secondary metabolite biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3unv, PDBe:3unv, PDBj:3unv
PDBsum3unv
PubMed22319000
UniProtQ84FL5

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