Structure of PDB 6lqy Chain A

Receptor sequence
>6lqyA (length=517) Species: 3755 (Prunus dulcis) [Search protein sequence]
HHHHLANTSAHDFSYLKFVYNATDTSLEGSYDYIVIGGGTSGCPLAATLS
EKYKVLLLERGTIATEYPNTLTADGFAYNLQQQDDGKTPVERFVSEDGID
NVRARILGGTTIINAGVYARANISFYSQTGIEWDLDLVNKTYEWVEDAIV
VKPNNQSWQSVIGEGFLEAGILPDNGFSLDHEAGTRLTGSTFDNNGTRHA
ADELLNKGDPNNLLVAVQASVEKILFSSNLSAIGVIYTDSDGNSHQAFVR
GNGEVIVSAGTIGTPQLLLLSGVGPESYLSSLNITVVQPNPYVGQFVYDN
PRNFINILPPNPIEASVVTVLGIRSDYYQVSLSSLPFSTPPFSLFPTTSY
PLPNSTFAHIVSQVPGPLSHGSVTLNSSSDVRIAPNIKFNYYSNSTDLAN
CVSGMKKLGDLLRTKALEPYKARDVLGIDGFNYLGVPLPTDDASFETFCL
DNVASYWHYHGGSLVGKVLDDSFRVMGIKALRVVDASTFPYEPNSHPQGF
YLMLGRYVGLQILQERS
3D structure
PDB6lqy Structure-Guided Tuning of a Hydroxynitrile Lyase to Accept Rigid Pharmaco Aldehydes.
ChainA
Resolution1.598 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.2.10: (R)-mandelonitrile lyase.
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 G33 T36 E55 R56 A100 G105 T106 N110 A111 V113 V217 A258 W459 H460 A488 H498 P499 Q500 G37 T40 E59 R60 A104 G109 T110 N114 A115 V117 V221 A259 W457 H458 A486 H496 P497 Q498
BS02 HBX A Y458 W459 H498 Y456 W457 H496
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
GO:0016829 lyase activity
GO:0046593 mandelonitrile lyase activity
GO:0050660 flavin adenine dinucleotide binding

View graph for
Molecular Function
External links
PDB RCSB:6lqy, PDBe:6lqy, PDBj:6lqy
PDBsum6lqy
PubMed
UniProtO24243|MDL1_PRUDU (R)-mandelonitrile lyase 1 (Gene Name=MDL1)

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