Structure of PDB 5eb4 Chain A

Receptor sequence
>5eb4A (length=515) Species: 3755 (Prunus dulcis) [Search protein sequence]
ANTSAHDFSYLKFVYNATDTSSEGSYDYIVIGGGTSGCPLAATLSEKYKV
LLLERGTIATEYPNTLTADGFAYNLQQQDDGKTPVERFVSEDGIDNVRAR
ILGGTTIINAGVYARANISFYSQTGIEWDLDLVNKTYEWVEDAIVVKPNN
QSWQSVIGEGFLEAGILPDNGFSLDHEAGTRLTGSTFDNNGTRHAADELL
NKGDPNNLLVAVQASVEKILFSSNLSAIGVIYTDSDGNSHQAFVRGNGEV
IVSAGTIGTPQLLLLSGVGPESYLSSLNITVVQPNPYVGQFVYDNPRNFI
NILPPNPIEASVATVLGIRSDYYQVSLSSLPFSTPPFSLFPTTSYPLPNS
TFAHIVSQVPGPLSHGSVTLNSSSDVRIAPNIKFNYYSNSTDLANCVSGM
KKLGDLLRTKALEPYKARDVLGIDGFNYLGVPLPENQTDDASFETFCLDN
VASYWHYHGGSLVGKVLDDSFRVMGIKALRVVDASTFPYEPNSHPQGFYL
MLGRYVGLQILQERS
3D structure
PDB5eb4 Structures of almond hydroxynitrile lyase isoenzyme 5 provide a rationale for the lack of oxidoreductase activity in flavin dependent HNLs.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V329 Q362 Y458 H460 S497 H498
Catalytic site (residue number reindexed from 1) V325 Q358 Y454 H456 S493 H494
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 G35 T36 E55 R56 A100 T106 N110 A111 V113 V217 A258 W459 H460 A488 H498 P499 Q500 G32 G34 T35 E54 R55 A99 T105 N109 A110 V112 V216 A254 W455 H456 A484 H494 P495 Q496
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:5eb4, PDBe:5eb4, PDBj:5eb4
PDBsum5eb4
PubMed27067080
UniProtO24243|MDL1_PRUDU (R)-mandelonitrile lyase 1 (Gene Name=MDL1)

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