3AKI
Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-L-arabinofuranosyl azido
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005576 | cellular_component | extracellular region |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0031222 | biological_process | arabinan catabolic process |
A | 0046373 | biological_process | L-arabinose metabolic process |
A | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:20739278 |
Chain | Residue | Details |
A | ASP20 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:20739278 |
Chain | Residue | Details |
A | GLU196 |
site_id | SWS_FT_FI3 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20739278 |
Chain | Residue | Details |
A | ASN159 | |
A | HIS260 | |
A | ARG294 | |
A | HIS336 | |
A | ASP352 | |
A | HIS430 | |
A | ASP448 |
site_id | SWS_FT_FI4 |
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:20739278 |
Chain | Residue | Details |
A | ASP135 |