Structure of PDB 1ju2 Chain A

Receptor sequence
>1ju2A (length=521) Species: 3755 (Prunus dulcis) [Search protein sequence]
LATTSDHDFSYLSFAYDATDLELEGSYDYVIVGGGTSGCPLAATLSEKYK
VLVLERGSLPTAYPNVLTADGFVYNLQQEDDGKTPVERFVSEDGIDNVRG
RVLGGTSIINAGVYARANTSIYSASGVDWDMDLVNQTYEWVEDTIVYKPN
SQSWQSVTKTAFLEAGVHPNHGFSLDHEEGTRITGSTFDNKGTRHAADEL
LNKGNSNNLRVGVHASVEKIIFSNAPGLTATGVIYRDSNGTPHQAFVRSK
GEVIVSAGTIGTPQLLLLSGVGPESYLSSLNIPVVLSHPYVGQFLHDNPR
NFINILPPNPIEPTIVTVLGISNDFYQCSFSSLPFTTPPFGFFPSSSYPL
PNSTFAHFASKVAGPLSYGSLTLKSSSNVRVSPNVKFNYYSNLTDLSHCV
SGMKKIGELLSTDALKPYKVEDLPGVEGFNILGIPLPKDQTDDAAFETFC
RESVASYWHYHGGCLVGKVLDGDFRVTGINALRVVDGSTFPYTPASHPQG
FYLMLGRYVGIKILQERSASD
3D structure
PDB1ju2 The hydroxynitrile lyase from almond: a lyase that looks like an oxidoreductase.
ChainA
Resolution1.47 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C328 K361 Y457 H459 S496 H497
Catalytic site (residue number reindexed from 1) C328 K361 Y457 H459 S496 H497
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 V98 G105 T106 N110 A111 V113 V217 A257 W458 H459 G487 H497 P498 Q499 Y502 G33 G35 T36 E55 R56 V98 G105 T106 N110 A111 V113 V217 A257 W458 H459 G487 H497 P498 Q499 Y502
Gene Ontology
Molecular Function
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
Biological Process
GO:0050898 nitrile metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1ju2, PDBe:1ju2, PDBj:1ju2
PDBsum1ju2
PubMed11566130
UniProtQ945K2|MDL2_PRUDU (R)-mandelonitrile lyase 2 (Gene Name=MDL2)

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