2DEP
Crystal Structure of xylanase B from Clostridium stercorarium F9
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008810 | molecular_function | cellulase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030245 | biological_process | cellulose catabolic process |
| A | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
| A | 0045493 | biological_process | xylan catabolic process |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008810 | molecular_function | cellulase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0030245 | biological_process | cellulose catabolic process |
| B | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
| B | 0045493 | biological_process | xylan catabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00591 |
| Number of Residues | 11 |
| Details | GH10_1 Glycosyl hydrolases family 10 (GH10) active site. GLDNiITELDM |
| Chain | Residue | Details |
| A | GLY286-MET296 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10061","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| A | HIS264 | |
| A | GLU185 | |
| A | GLU293 | |
| A | ASP295 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| B | HIS264 | |
| B | GLU185 | |
| B | GLU293 | |
| B | ASP295 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| A | GLU185 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| B | GLU185 |
