5H9O
Complex of Murine endoplasmic reticulum alpha-glucosidase II with D-Glucose
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 | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006491 | biological_process | N-glycan processing |
| A | 0015926 | molecular_function | glucosidase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0017177 | cellular_component | glucosidase II complex |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0033919 | molecular_function | glucan 1,3-alpha-glucosidase activity |
| A | 0042470 | cellular_component | melanosome |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0090599 | molecular_function | alpha-glucosidase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005515 | molecular_function | protein binding |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005794 | cellular_component | Golgi apparatus |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006491 | biological_process | N-glycan processing |
| C | 0015926 | molecular_function | glucosidase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0017177 | cellular_component | glucosidase II complex |
| C | 0030246 | molecular_function | carbohydrate binding |
| C | 0033919 | molecular_function | glucan 1,3-alpha-glucosidase activity |
| C | 0042470 | cellular_component | melanosome |
| C | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| C | 0090599 | molecular_function | alpha-glucosidase activity |
Functional Information from PROSITE/UniProt
| 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_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27462106, ECO:0007744|PDB:5HJO |
| Chain | Residue | Details |
| B | ASP49 | |
| B | ASP53 | |
| D | ASP49 | |
| D | ASP53 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27462106, ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O, ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR, ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE, ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG |
| Chain | Residue | Details |
| B | GLN50 | |
| B | ASP104 | |
| B | GLU105 | |
| D | GLN50 | |
| D | TYR55 | |
| D | ASP57 | |
| D | ASP63 | |
| D | GLU64 | |
| D | ARG91 | |
| D | ASP94 | |
| D | VAL96 | |
| B | TYR55 | |
| D | ASP98 | |
| D | ASP104 | |
| D | GLU105 | |
| B | ASP57 | |
| B | ASP63 | |
| B | GLU64 | |
| B | ARG91 | |
| B | ASP94 | |
| B | VAL96 | |
| B | ASP98 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKC => ECO:0000255 |
| Chain | Residue | Details |
| B | SER89 | |
| D | SER89 | |
| A | PRO679 | |
| A | VAL753 | |
| C | ALA341 | |
| C | ARG506 | |
| C | PRO679 | |
| C | VAL753 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| B | ASN72 | |
| D | ASN72 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10921916, ECO:0000269|PubMed:27462106, ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR, ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE, ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG |
| Chain | Residue | Details |
| A | ASN97 | |
| C | ASN97 |
