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 | 0008152 | biological_process | 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 |
Functional Information from PDB Data
site_id | ABC |
Number of Residues | 1 |
Details | THE ACID BASE CATALYST IS RESIDUE GLU 172. |
site_id | NUC |
Number of Residues | 1 |
Details | THE NUCLEOPHILE TO WHICH THE INHIBITOR IS BOUND IS GLU 78. |
Functional Information from PROSITE/UniProt
site_id | PS00776 |
Number of Residues | 11 |
Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW |
Chain | Residue | Details |
A | PRO75-TRP85 | |
site_id | PS00777 |
Number of Residues | 12 |
Details | GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS |
Chain | Residue | Details |
A | MET169-SER180 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU78 | |
Chain | Residue | Details |
A | GLU172 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 432 |
Chain | Residue | Details |
A | ASN35 | modifies pKa |
A | TYR69 | electrostatic destabiliser |
A | GLU78 | covalent catalysis, proton shuttle (general acid/base) |
A | TYR80 | modifies pKa |
A | GLU172 | proton shuttle (general acid/base) |