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 | 0046558 | molecular_function | arabinan endo-1,5-alpha-L-arabinosidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CA A 502 |
Chain | Residue |
A | HOH2008 |
A | HOH2014 |
A | HOH2108 |
A | HOH2110 |
A | HOH2160 |
A | HOH2203 |
A | HOH2204 |
A | HOH2275 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A1294 |
Chain | Residue |
A | GLU135 |
A | ASP257 |
A | HOH2111 |
A | HOH2161 |
A | HOH2299 |
A | HOH2300 |
A | ASP77 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 604 |
Chain | Residue |
A | HOH2296 |
A | HOH2297 |
A | HOH2298 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A1295 |
Chain | Residue |
A | ASP244 |
A | GLY246 |
A | ASN247 |
A | TRP250 |
A | ARG266 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A1296 |
Chain | Residue |
A | LYS156 |
A | LEU171 |
A | SER173 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO A1297 |
Chain | Residue |
A | MET17 |
A | ILE18 |
A | ILE78 |
A | GLN79 |
A | VAL259 |
A | ASN260 |
A | HOH2299 |
A | HOH2300 |
A | HOH2301 |
A | HOH2302 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP14 | |
Chain | Residue | Details |
A | GLU185 | |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP14 | |
A | GLY95 | |
A | ASN130 | |
A | SER150 | |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | ASP77 | |
A | GLU135 | |
A | ASP257 | |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate => ECO:0000305|PubMed:15708971 |
Chain | Residue | Details |
A | ASP133 | |