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Structure of PDB 1e4m Chain M

Receptor sequence
>1e4mM (length=499) Species: 3728 (Sinapis alba) [Search protein sequence]
EITCQENLPFTCGNTDALNSSSFSSDFIFGVASSAYQIEGTIGRGLNIWD
GFTHRYPNKSGPDHGNGDTTCDSFSYWQKDIDVLDELNATGYRFSIAWSR
IIPRGKRSRGVNEKGIDYYHGLISGLIKKGITPFVTLFHWDLPQTLQDEY
EGFLDPQIIDDFKDYADLCFEEFGDSVKYWLTINQLYSVPTRGYGSALDA
PGRCSPTVDPSCYAGNSSTEPYIVAHHQLLAHAKVVDLYRKNYTHQGGKI
GPTMITRWFLPYNDTDRHSIAATERMKEFFLGWFMGPLTNGTYPQIMIDT
VGERLPSFSPEESNLVKGSYDFLGLNYYFTQYAQPSPNPVNSTNHTAMMD
AGAKLTYINASGHYIGPLFEKDKADSTDNIYYYPKGIYSVMDYFKNKYYN
PLIYVTENGISTPGDENRNQSMLDYTRIDYLCSHLCFLNKVIKEKDVNVK
GYLAWALGDNYEFNKGFTVRFGLSYIDWNNVTDRDLKKSGQWYQSFISP
3D structure
PDB1e4m High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base
ChainM
Resolution1.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.147: thioglucosidase.
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 ZN M H56 D70 H54 D68
BS02 SO4 M K108 R111 K106 R109
BS03 SO4 M H270 A273 H268 A271
BS04 SO4 M N60 H66 N58 H64
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0019137 thioglucosidase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009651 response to salt stress
GO:0019762 glucosinolate catabolic process
Cellular Component
GO:0005773 vacuole

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Cellular Component
External links
PDB RCSB:1e4m, PDBe:1e4m, PDBj:1e4m
PDBsum1e4m
PubMed10978344
UniProtP29736|MYRA_SINAL Myrosinase MA1

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