6T13
CRYSTAL STRUCTURE OF GLUCOCEREBROSIDASE IN COMPLEX WITH A PYRROLOPYRAZINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004348 | molecular_function | glucosylceramidase activity |
| A | 0006665 | biological_process | sphingolipid metabolic process |
| B | 0004348 | molecular_function | glucosylceramidase activity |
| B | 0006665 | biological_process | sphingolipid metabolic process |
| C | 0004348 | molecular_function | glucosylceramidase activity |
| C | 0006665 | biological_process | sphingolipid metabolic process |
| D | 0004348 | molecular_function | glucosylceramidase activity |
| D | 0006665 | biological_process | sphingolipid metabolic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15817452","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15817452","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12792654","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17139081","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17139081","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17139081","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 764 |
| Chain | Residue | Details |
| A | GLU235 | activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| A | GLU340 | covalently attached, nucleofuge, nucleophile |
| A | CYS342 | electrostatic stabiliser |
| A | ASN370 |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 764 |
| Chain | Residue | Details |
| B | GLU235 | activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| B | GLU340 | covalently attached, nucleofuge, nucleophile |
| B | CYS342 | electrostatic stabiliser |
| B | ASN370 |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 764 |
| Chain | Residue | Details |
| C | GLU235 | activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| C | GLU340 | covalently attached, nucleofuge, nucleophile |
| C | CYS342 | electrostatic stabiliser |
| C | ASN370 |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 764 |
| Chain | Residue | Details |
| D | GLU235 | activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| D | GLU340 | covalently attached, nucleofuge, nucleophile |
| D | CYS342 | electrostatic stabiliser |
| D | ASN370 |
