Structure of PDB 3red Chain C

Receptor sequence
>3redC (length=521) Species: 102107 (Prunus mume) [Search protein sequence]
LATTSDHDFSYLSFAYDATDLELEGSYDYVIVGGGTSGCPLAATLSEKYK
VLVLERGTLPTAYPNLLTSDGFIYNLQQEDDGQTPVERFVSGDGIDDVRG
RVLGGTSMINAGVYARANTKIFSASGIEWDMDLVNQTYDWVEDTIVYKPD
KQAWQSLTKTAFLEAGVLPDNGFSLDHEAGTRLTGSTFDNNGTRHASDEL
LNKGDPNNLRVAVHASVEKIIFSSNSSGVTAIGVIYKDSNGTPHQAFVRG
EGEVIVSAGPIGSPQLLLLSGVGPESYLSSLNIPVVLSHPYVGQFLHDNP
RNFINILPPNPIEPSTVTVLGITSNFYQCSFSSLPFSIPPFAFFPNPTYP
LPNSTFAHFVNKVPGPLSYGSITLNSDSDVRVAPNVKFNYYSNSTDLAHC
VSGMKKIGELLSSDALKPYKVEDLPGIDGFDILGIPLPENQTDDAAFETF
CREAVASYWHYHGGCLVGEVLDGDFRVTGINALRVVDGSTFPYSPASHPQ
GFYLMLGRYVGSKILQERSAA
3D structure
PDB3red Crystal Structure of a native FAD-dependent Hydroxynitrile Lyase derived from the Japanese apricot, Prunus mume
ChainC
Resolution3.03 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C329 K362 Y458 H460 S497 H498
Catalytic site (residue number reindexed from 1) C329 K362 Y458 H460 S497 H498
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 C G33 T36 E55 R56 G105 T106 N110 A111 V113 V217 A258 W459 H460 D487 G488 H498 P499 Q500 G33 T36 E55 R56 G105 T106 N110 A111 V113 V217 A258 W459 H460 D487 G488 H498 P499 Q500
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:3red, PDBe:3red, PDBj:3red
PDBsum3red
PubMed
UniProtB9X0I1

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