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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PGE A 501 |
Chain | Residue |
A | LYS195 |
A | ASN198 |
A | VAL208 |
A | GLU209 |
A | SER211 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 A 502 |
Chain | Residue |
A | ASN102 |
A | ARG105 |
A | HIS109 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 503 |
Chain | Residue |
A | GLU399 |
A | LYS395 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 504 |
Chain | Residue |
A | VAL193 |
A | LYS197 |
A | GLU245 |
A | HOH767 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 505 |
Chain | Residue |
A | PRO321 |
A | PRO323 |
A | HOH819 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 506 |
Chain | Residue |
A | TRP99 |
A | ALA100 |
A | ARG105 |
A | ASN238 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 507 |
Chain | Residue |
A | THR229 |
A | ASN276 |
A | HIS450 |
A | HIS452 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT A 508 |
Chain | Residue |
A | LEU256 |
A | PRO257 |
A | VAL259 |
A | ARG295 |
A | ALA296 |
A | HOH729 |
A | HOH765 |
Functional Information from PROSITE/UniProt
site_id | PS00655 |
Number of Residues | 17 |
Details | GLYCOSYL_HYDROL_F6_1 Glycosyl hydrolases family 6 signature 1. VvYdlPdRDCAalASnG |
Chain | Residue | Details |
A | VAL168-GLY184 | |
site_id | PS00656 |
Number of Residues | 10 |
Details | GLYCOSYL_HYDROL_F6_2 Glycosyl hydrolases family 6 signature 2. LLVIEPDSLA |
Chain | Residue | Details |
A | LEU216-ALA225 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | THR117 | |
Chain | Residue | Details |
A | SER126 | |
Chain | Residue | Details |
A | ASP222 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
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 | ASP176 | |
Chain | Residue | Details |
A | ASN290 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 440 |
Chain | Residue | Details |
A | TYR170 | modifies pKa, steric role |
A | ARG175 | electrostatic stabiliser |
A | ASP176 | modifies pKa, proton shuttle (general acid/base), transition state stabiliser |
A | SER182 | electrostatic stabiliser |
A | ASP222 | proton shuttle (general acid/base) |
A | ASP401 | electrostatic stabiliser |