Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0030245 | biological_process | cellulose catabolic process |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0030245 | biological_process | cellulose catabolic process |
Functional Information from PDB Data
site_id | ST1 |
Number of Residues | 3 |
Details | CATALYTIC SITE INCLUDING MUTATED TYR-> PHE. |
Chain | Residue |
A | ASP175 |
A | ASP221 |
A | PHE169 |
site_id | ST2 |
Number of Residues | 3 |
Details | CATALYTIC SITE INCLUDING MUTATED TYR-> PHE. |
Chain | Residue |
B | ASP175 |
B | ASP221 |
B | PHE169 |
Functional Information from PROSITE/UniProt
site_id | PS00656 |
Number of Residues | 10 |
Details | GLYCOSYL_HYDROL_F6_2 Glycosyl hydrolases family 6 signature 2. LLVIEPDSLA |
Chain | Residue | Details |
A | LEU215-ALA224 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP221 | |
B | ASP221 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer that also modulates the pKa of Asp-245 and may act as a proton acceptor through a water chain => ECO:0000269|PubMed:2377893 |
Chain | Residue | Details |
A | ASP175 | |
B | ASP175 | |
Chain | Residue | Details |
A | THR87 | |
A | THR97 | |
A | THR122 | |
B | THR87 | |
B | THR97 | |
B | THR122 | |
Chain | Residue | Details |
A | SER106 | |
A | SER109 | |
A | SER110 | |
A | SER115 | |
B | SER106 | |
B | SER109 | |
B | SER110 | |
B | SER115 | |
Chain | Residue | Details |
A | ASN289 | |
B | ASN289 | |
Chain | Residue | Details |
A | ASN310 | |
B | ASN310 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qk2 |
Chain | Residue | Details |
A | ASP175 | |
A | ASP221 | |
A | PHE169 | |
A | ARG174 | |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qk2 |
Chain | Residue | Details |
B | ASP175 | |
B | ASP221 | |
B | PHE169 | |
B | ARG174 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qk2 |
Chain | Residue | Details |
A | ASP221 | |
A | ASP401 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qk2 |
Chain | Residue | Details |
B | ASP221 | |
B | ASP401 | |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 440 |
Chain | Residue | Details |
A | PHE169 | modifies pKa, steric role |
A | ARG174 | electrostatic stabiliser |
A | ASP175 | modifies pKa, proton shuttle (general acid/base), transition state stabiliser |
A | SER181 | electrostatic stabiliser |
A | ASP221 | proton shuttle (general acid/base) |
A | ASP401 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 440 |
Chain | Residue | Details |
B | PHE169 | modifies pKa, steric role |
B | ARG174 | electrostatic stabiliser |
B | ASP175 | modifies pKa, proton shuttle (general acid/base), transition state stabiliser |
B | SER181 | electrostatic stabiliser |
B | ASP221 | proton shuttle (general acid/base) |
B | ASP401 | electrostatic stabiliser |