Structure of PDB 4atl Chain B

Receptor sequence
>4atlB (length=470) Species: 4060 (Rauvolfia serpentina) [Search protein sequence]
NDATRISRSDFPADFIMGTGSSAYQIEGGARDGGRGPSIWDTFTHRRPDM
IRGGTNGDVAVDSYHLYKEDVNILKNLGLDAYRFSISWSRVLPGGRLSGG
VNKEGINYYNNLIDGLLANGIKPFVTLFHWDVPQALEDEYGGFLSPRIVD
DFCEYAELCFWEFGDRVKHWMTLNEPWTFSVHGYATGLYAPGRGRSTGNP
GTEPYWVTHHLLLAHAAAVELYKNKFQRGQEGQIGISHATQWMEPWDENS
ASDVEAAARALDFMLGWFMEPITSGDYPKSMKKFVGSRLPKFSPEQSKML
KGSYDFVGLNYYTASYVTNASNFSYNTDIHVTYETDRNGVPIGPQSGSDW
LLIYPEGIRKILVYTKKTYNVPLIYVTENGVDDVKNTNLTLSEARKDSMR
LKYLQDHIFNVRQAMNDGVNVKGYFAWSLLDNFEWGEGYGVRFGIIHIDY
NDNFARYPKDSAVWLMNSFH
3D structure
PDB4atl High Speed X-Ray Analysis of Plant Enzymes at Room Temperature
ChainB
Resolution2.52 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 E186 T189 N345 Y347 E420
Catalytic site (residue number reindexed from 1) R83 H129 E175 T178 N310 Y312 E378
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 B Q36 H140 E186 E420 W469 E476 W477 F485 Q25 H129 E175 E378 W427 E434 W435 F443
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
View graph for
Biological Process
External links
PDB RCSB:4atl, PDBe:4atl, PDBj:4atl
PDBsum4atl
PubMed22704651
UniProtQ9SPP9|RG1_RAUSE Raucaffricine-O-beta-D-glucosidase (Gene Name=RG)

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