5H4U
Crystal structure of cellulase from Antarctic springtail, Cryptopygus antarcticus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008810 | molecular_function | cellulase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008810 | molecular_function | cellulase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0008810 | molecular_function | cellulase activity |
Functional Information from PROSITE/UniProt
| site_id | PS01140 |
| Number of Residues | 12 |
| Details | GLYCOSYL_HYDROL_F45 Glycosyl hydrolases family 45 active site. TTRYWDcckpsC |
| Chain | Residue | Details |
| A | THR8-CYS19 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10069","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28156112","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"28156112","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
