Structure of PDB 1e4m Chain M

Receptor sequence

>1e4mM (length=499) Species: 3728 (Sinapis alba)

EITCQENLPFTCGNTDALNSSSFSSDFIFGVASSAYQIEGTIGRGLNIWD
GFTHRYPNKSGPDHGNGDTTCDSFSYWQKDIDVLDELNATGYRFSIAWSR
IIPRGKRSRGVNEKGIDYYHGLISGLIKKGITPFVTLFHWDLPQTLQDEY
EGFLDPQIIDDFKDYADLCFEEFGDSVKYWLTINQLYSVPTRGYGSALDA
PGRCSPTVDPSCYAGNSSTEPYIVAHHQLLAHAKVVDLYRKNYTHQGGKI
GPTMITRWFLPYNDTDRHSIAATERMKEFFLGWFMGPLTNGTYPQIMIDT
VGERLPSFSPEESNLVKGSYDFLGLNYYFTQYAQPSPNPVNSTNHTAMMD
AGAKLTYINASGHYIGPLFEKDKADSTDNIYYYPKGIYSVMDYFKNKYYN
PLIYVTENGISTPGDENRNQSMLDYTRIDYLCSHLCFLNKVIKEKDVNVK
GYLAWALGDNYEFNKGFTVRFGLSYIDWNNVTDRDLKKSGQWYQSFISP

3D structure

• PDB: 1e4m High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base
• Chain: M
• Resolution: 1.2 Å

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

External links

• PDB: RCSB:1e4m, PDBe:1e4m, PDBj:1e4m
• PDBsum: 1e4m
• PubMed: 10978344
• UniProt: P29736|MYRA_SINAL Myrosinase MA1