1MYR
MYROSINASE FROM SINAPIS ALBA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005773 | cellular_component | vacuole |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008422 | molecular_function | beta-glucosidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0019137 | molecular_function | thioglucosidase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | ASN |
| Number of Residues | 2 |
| Details | ACTIVE SITE NUCLEOPHILE AT THE POSITION OF THE GENERAL ACID/BASE |
| Chain | Residue |
| A | GLU409 |
| A | GLN187 |
| site_id | ZNB |
| Number of Residues | 2 |
| Details | ZN BINDING SITE TOGETHER WITH THE SYMMETRY-RELATED EQUIVALENTS. |
| Chain | Residue |
| A | HIS56 |
| A | ASP70 |
Functional Information from PROSITE/UniProt
| site_id | PS00572 |
| Number of Residues | 9 |
| Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYVTENGIS |
| Chain | Residue | Details |
| A | ILE405-SER413 |
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FiFGvAsSAYQiEgT |
| Chain | Residue | Details |
| A | PHE29-THR43 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10978344","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 11 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10978344","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15889170","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9195886","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 9195886, 16291087 |
| Chain | Residue | Details |
| A | GLN187 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 460 |
| Chain | Residue | Details |
| A | ARG95 | electrostatic stabiliser |
| A | GLN187 | electrostatic stabiliser, modifies pKa, steric role |
| A | SER190 | electrostatic stabiliser, steric role |
| A | ASN328 | electrostatic stabiliser, steric role |
| A | TYR330 | transition state stabiliser |
| A | GLU409 | covalently attached, electrostatic stabiliser |
