Structure of PDB 1myr Chain A Binding Site BS01

Receptor Information
>1myr Chain A (length=499) Species: 3728 (Sinapis alba) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EITCQENNPFTCGNTDGLNSSSFEADFIFGVASSAYQIEGTIGRGLNIWD
GFTHRYPDKSGPDHGNGDTTCDSFSYWQKDIDVLDELNATGYRFSIAWSR
IIPRGKRSRGVNQKGIDYYHGLIDGLIKKGITPFVTLFHWDLPQTLQDEY
EGFLDPQIIDDFKDYADLCFEEFGDSVKYWLTINQLYSVPTRGYGSALDA
PGRCSPTVDPSCYAGNSSTEPYIVAHHQLLAHAKVVDLYRKNYTHQGGKI
GPTMITRWFLPYNDTDRHSIAATERMKQFFLGWFMGPLTNGTYPQIMIDT
VGARLPTFSPEETNLVKGSYDFLGLNYYFTQYAQPSPNPVNATNHTAMMD
AGAKLTYINASGHYIGPLFESDGGDGSSNIYYYPKGIYSVMDYFKNKYYN
PLIYVTENGISTPGSENRKESMLDYTRIDYLCSHLCFLNKVIKEKDVNVK
GYLAWALGDNYEFNNGFTVRFGLSYINWNNVTDRDLKKSGQWYQKFISP
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1myr Chain A Residue 992 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1myr The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase.
Resolution1.64 Å
Binding residue
(original residue number in PDB)		H56 D70
Binding residue
(residue number reindexed from 1)		H54 D68
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) R95 H141 Q187 S190 N328 Y330 E409
Catalytic site (residue number reindexed from 1) R93 H139 Q185 S188 N326 Y328 E407
Enzyme Commision number 3.2.1.147: thioglucosidase.
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1myr, PDBe:1myr, PDBj:1myr
PDBsum1myr
PubMed9195886
UniProtP29736|MYRA_SINAL Myrosinase MA1

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