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 | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10069, ECO:0000305|PubMed:28156112 |
Chain | Residue | Details |
A | ASP13 | |
B | ASP13 | |
C | ASP13 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:28156112 |
Chain | Residue | Details |
A | ASP122 | |
B | ASP122 | |
C | ASP122 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ASN39 | |
B | ASN39 | |
C | ASN39 |