Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004339 | molecular_function | glucan 1,4-alpha-glucosidase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005976 | biological_process | polysaccharide metabolic process |
Functional Information from PDB Data
| site_id | ACT |
| Number of Residues | 4 |
| Details | ACTIVE SITE: RESIDUES THAT BIND ACARBOSE AND 1-DEOXYNOJIRIMYCIN AT SUBSITE 1 OF THE ACTIVE SITE ARE OD1 ASP 55, OD2 ASP 55, NH1 ARG 305, CARBONYL 177, NE ARG 54, AND NH2 ARG 54. GLU 179 IS THE CATALYTIC ACID AND RESIDUE GLU 400 IS THE CATALYTIC BASE. WATER 500 IS THE NUCLEOPHILE. |
| Chain | Residue |
| A | ASP55 |
| A | ARG305 |
| A | LEU177 |
| A | ARG54 |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DKSDGDELSarDL |
| Chain | Residue | Details |
| A | ASP403-LEU415 | |
| site_id | PS00820 |
| Number of Residues | 11 |
| Details | GLUCOAMYLASE Glucoamylase active site region signature. TGy.DlWEEvnG |
| Chain | Residue | Details |
| A | THR173-GLY183 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10051","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1970434","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10051","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1970434","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000112"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000113"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"O-linked (Man) serine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 5 |
| Details | Glycosylation: {"description":"O-linked (Man) serine"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"O-linked (Man) threonine"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1agm |
| Chain | Residue | Details |
| A | GLU179 | |
| A | GLU400 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 393 |
| Chain | Residue | Details |
| A | TRP120 | transition state stabiliser |
| A | ASP176 | proton shuttle (general acid/base), transition state stabiliser |
| A | GLU179 | proton shuttle (general acid/base) |
| A | GLU180 | activator |
| A | GLU400 | activator |
