7JTY
Co-crystal structure of alpha glucosidase with compound 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0030246 | molecular_function | carbohydrate binding |
| B | 0001701 | biological_process | in utero embryonic development |
| B | 0001889 | biological_process | liver development |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005080 | molecular_function | protein kinase C binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0006491 | biological_process | N-glycan processing |
| B | 0010977 | biological_process | negative regulation of neuron projection development |
| B | 0017177 | cellular_component | glucosidase II complex |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0044325 | molecular_function | transmembrane transporter binding |
| B | 0044877 | molecular_function | protein-containing complex binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051219 | molecular_function | phosphoprotein binding |
| B | 0071941 | biological_process | nitrogen cycle metabolic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0030246 | molecular_function | carbohydrate binding |
| D | 0001701 | biological_process | in utero embryonic development |
| D | 0001889 | biological_process | liver development |
| D | 0003723 | molecular_function | RNA binding |
| D | 0005080 | molecular_function | protein kinase C binding |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0006491 | biological_process | N-glycan processing |
| D | 0010977 | biological_process | negative regulation of neuron projection development |
| D | 0017177 | cellular_component | glucosidase II complex |
| D | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| D | 0044325 | molecular_function | transmembrane transporter binding |
| D | 0044877 | molecular_function | protein-containing complex binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051219 | molecular_function | phosphoprotein binding |
| D | 0071941 | biological_process | nitrogen cycle metabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DDNMDGMVSlaEL |
| Chain | Residue | Details |
| B | ASP222-LEU234 |
| site_id | PS00129 |
| Number of Residues | 8 |
| Details | GLYCOSYL_HYDROL_F31_1 Glycosyl hydrolases family 31 active site. YVWnDMNE |
| Chain | Residue | Details |
| A | TYR560-GLU567 |
| site_id | PS00707 |
| Number of Residues | 31 |
| Details | GLYCOSYL_HYDROL_F31_2 Glycosyl hydrolases family 31 signature 2. GADVGGFfknPepeLLvRWyqMGAYqPFfRA |
| Chain | Residue | Details |
| A | GLY667-ALA697 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5HJR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5HJO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q14697","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10921916","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5F0E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5HJO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5HJR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IED","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 68 |
| Details | Domain: {"description":"LDL-receptor class A 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 88 |
| Details | Domain: {"description":"LDL-receptor class A 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5HJO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27462106","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5F0E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5H9O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5HJO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5HJR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IED","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IEG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
