Structure of PDB 4ek7 Chain A

Receptor sequence
>4ek7A (length=470) Species: 4060 (Rauvolfia serpentina) [Search protein sequence]
DATRISRSDFPADFIMGTGSSAYQIEGGARDGGRGPSIWDTFTHRRPDMI
RGGTNGDVAVDSYHLYKEDVNILKNLGLDAYRFSISWSRVLPGGRLSGGV
NKEGINYYNNLIDGLLANGIKPFVTLFHWDVPQALEDEYGGFLSPRIVDD
FCEYAELCFWEFGDRVKHWMTLNQPWTFSVHGYATGLYAPGRGRSTGNPG
TEPYWVTHHLLLAHAAAVELYKNKFQRGQEGQIGISHATQWMEPWDENSA
SDVEAAARALDFMLGWFMEPITSGDYPKSMKKFVGSRLPKFSPEQSKMLK
GSYDFVGLNYYTASYVTNASNFSYNTDIHVTYETDRNGVPIGPQSGSDWL
LIYPEGIRKILVYTKKTYNVPLIYVTENGVDDVKNTNLTLSEARKDSMRL
KYLQDHIFNVRQAMNDGVNVKGYFAWSLLDNFEWGEGYGVRFGIIHIDYN
DNFARYPKDSAVWLMNSFHK
3D structure
PDB4ek7 High speed X-ray analysis of plant enzymes at room temperature.
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) R94 H140 Q186 T189 N345 Y347 E420
Catalytic site (residue number reindexed from 1) R82 H128 Q174 T177 N309 Y311 E377
Enzyme Commision number 2.4.1.219: vomilenine glucosyltransferase.
3.2.1.125: raucaffricine beta-glucosidase.
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 BGC A Q36 Q186 Y347 E420 W469 E476 W477 Q24 Q174 Y311 E377 W426 E433 W434
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016740 transferase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0050247 raucaffricine beta-glucosidase activity
GO:0050506 vomilenine glucosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009820 alkaloid metabolic process
GO:0009821 alkaloid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4ek7, PDBe:4ek7, PDBj:4ek7
PDBsum4ek7
PubMed22704651
UniProtQ9SPP9|RG1_RAUSE Raucaffricine-O-beta-D-glucosidase (Gene Name=RG)

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