1AQ0
BARLEY 1,3-1,4-BETA-GLUCANASE IN MONOCLINIC SPACE GROUP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0042972 | molecular_function | licheninase activity |
| A | 0042973 | molecular_function | glucan endo-1,3-beta-D-glucosidase activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0042972 | molecular_function | licheninase activity |
| B | 0042973 | molecular_function | glucan endo-1,3-beta-D-glucosidase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00587 |
| Number of Residues | 14 |
| Details | GLYCOSYL_HYDROL_F17 Glycosyl hydrolases family 17 signature. VkLVVSESGWPSgG |
| Chain | Residue | Details |
| A | VAL226-GLY239 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O22317","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"O22317","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 9452466 |
| Chain | Residue | Details |
| A | GLU280 | |
| A | LYS283 | |
| A | GLU288 | |
| A | GLU232 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 9452466 |
| Chain | Residue | Details |
| B | GLU280 | |
| B | LYS283 | |
| B | GLU288 | |
| B | GLU232 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 400 |
| Chain | Residue | Details |
| A | GLU232 | covalent catalysis |
| A | GLU280 | electrostatic stabiliser |
| A | LYS283 | electrostatic stabiliser |
| A | GLU288 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 400 |
| Chain | Residue | Details |
| B | GLU232 | covalent catalysis |
| B | GLU280 | electrostatic stabiliser |
| B | LYS283 | electrostatic stabiliser |
| B | GLU288 | proton shuttle (general acid/base) |
