6FRV
Structure of the catalytic domain of Aspergillus niger Glucoamylase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0000324 | cellular_component | fungal-type vacuole |
| A | 0004339 | molecular_function | glucan 1,4-alpha-glucosidase activity |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005976 | biological_process | polysaccharide metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 2001070 | molecular_function | starch binding |
Functional Information from PROSITE/UniProt
| site_id | PS00820 |
| Number of Residues | 11 |
| Details | GLUCOAMYLASE Glucoamylase active site region signature. TGy.DlWEEvnG |
| Chain | Residue | Details |
| A | THR197-GLY207 |
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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10051","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 7 |
| Details | Glycosylation: {"description":"O-linked (Man) serine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1983","firstPage":"529","lastPage":"544","volume":"48","journal":"Carlsberg Res. Commun.","title":"The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger.","authors":["Svensson B.","Larsen K.","Svendsen I.","Boel E."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"O-linked (Man) threonine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1983","firstPage":"529","lastPage":"544","volume":"48","journal":"Carlsberg Res. Commun.","title":"The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger.","authors":["Svensson B.","Larsen K.","Svendsen I.","Boel E."]}}]} |
| Chain | Residue | Details |
