1REE
ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 3,4-EPOXYBUTYL-BETA-D-XYLOSIDE
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 | 0005576 | cellular_component | extracellular region | 
| A | 0005975 | biological_process | carbohydrate metabolic process | 
| A | 0016787 | molecular_function | hydrolase activity | 
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds | 
| 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 | 0005576 | cellular_component | extracellular region | 
| B | 0005975 | biological_process | carbohydrate metabolic process | 
| B | 0016787 | molecular_function | hydrolase activity | 
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds | 
| B | 0031176 | molecular_function | endo-1,4-beta-xylanase activity | 
| B | 0045493 | biological_process | xylan catabolic process | 
Functional Information from PROSITE/UniProt
| site_id | PS00776 | 
| Number of Residues | 11 | 
| Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYIVEnF | 
| Chain | Residue | Details | 
| A | PRO83-PHE93 | 
| site_id | PS00777 | 
| Number of Residues | 12 | 
| Details | GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. VavEGYFSSGsA | 
| Chain | Residue | Details | 
| A | VAL174-ALA185 | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 2 | 
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"26392527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000305"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 2 | 
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"26392527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000305"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 14 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 4 | 
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} | 
| Chain | Residue | Details | 
Catalytic Information from CSA
| site_id | CSA1 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1bvv | 
| Chain | Residue | Details | 
| A | GLU177 | |
| A | GLU86 | 
| site_id | CSA2 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1bvv | 
| Chain | Residue | Details | 
| B | GLU177 | |
| B | GLU86 | 






