Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0016787 | molecular_function | hydrolase activity |
A | 0030245 | biological_process | cellulose catabolic process |
A | 0045493 | biological_process | xylan catabolic process |
A | 0046555 | molecular_function | acetylxylan esterase activity |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 209 |
Chain | Residue |
A | THR146 |
A | ASP172 |
A | ALA173 |
A | SER174 |
site_id | CAT |
Number of Residues | 3 |
Details | THESE RESIDUES FORM THE CATALYTIC TRIAD. |
Chain | Residue |
A | SER90 |
A | ASP175 |
A | HIS187 |
Functional Information from PROSITE/UniProt
site_id | PS00120 |
Number of Residues | 10 |
Details | LIPASE_SER Lipases, serine active site. IVLVGYSQGG |
Chain | Residue | Details |
A | ILE84-GLY93 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | SER90 | |
A | ASP175 | |
A | HIS187 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN180 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1bs9 |
Chain | Residue | Details |
A | THR13 | |
A | ASP175 | |
A | SER90 | |
A | HIS187 | |
A | GLN91 | |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 431 |
Chain | Residue | Details |
A | THR13 | electrostatic stabiliser |
A | SER90 | covalent catalysis, proton shuttle (general acid/base) |
A | GLN91 | steric role |
A | ASP175 | modifies pKa |
A | HIS187 | proton shuttle (general acid/base) |