Structure of PDB 2ylz Chain A

Receptor sequence
>2ylzA (length=533) Species: 2021 (Thermobifida fusca) [Search protein sequence]
RRQPPEEVDVLVVGAGFSGLYALYRLRELGRSVHVIETAGDVGGVWYWNR
YPGARCDIESIEYCYSFSEEVLQEWNWTERYASQPEILRYINFVADKFDL
RSGITFHTTVTAAAFDEATNTWTVDTNHGDRIRARYLIMASGQLSVPQLP
NFPGLKDFAGNLYHTGNWPHEPVDFSGQRVGVIGTGSSGIQVSPQIAKQA
AELFVFQRTPHFAVPARNAPLDPEFLADLKKRYAEFREESRNTPGGTHRY
QGPKSALEVSDEELVETLERYWQEGGPDILAAYRDILRDRDANERVAEFI
RNKIRNTVRDPEVAERLVPKGYPFGTKRLILEIDYYEMFNRDNVHLVDTL
SAPIETITPRGVRTSEREYELDSLVLATGFDALTGALFKIDIRGVGNVAL
KEKWAAGPRTYLGLSTAGFPNLFFIAGPGSPSALSNGLVSIEQHVEWVTD
HIAYMFKNGLTRSEAVLEKEDEWVEHVNEIADETLYPMTASWYTGANVPG
KPRVFMLYVGGFHRYRQICDEVAAKGYEGFVLT
3D structure
PDB2ylz Snapshots of Enzymatic Baeyer-Villiger Catalysis: Oxygen Activation and Intermediate Stabilization.
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.13.92: phenylacetone monooxygenase.
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 FAD A V22 G23 G25 S27 E46 T47 G53 V54 W55 C65 D66 I67 Y72 T118 V119 S150 G151 Q152 R337 I399 G446 V13 G14 G16 S18 E37 T38 G44 V45 W46 C56 D57 I58 Y63 T109 V110 S141 G142 Q143 R328 I390 G437
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0004499 N,N-dimethylaniline monooxygenase activity
GO:0016709 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
GO:0033776 phenylacetone monooxygenase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0050661 NADP binding

View graph for
Molecular Function
External links
PDB RCSB:2ylz, PDBe:2ylz, PDBj:2ylz
PDBsum2ylz
PubMed21697090
UniProtQ47PU3|PAMO_THEFY Phenylacetone monooxygenase (Gene Name=pamO)

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