1GYE
Structure of Cellvibrio cellulosa alpha-L-arabinanase complexed with Arabinohexaose
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005576 | cellular_component | extracellular region |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008152 | biological_process | metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0031222 | biological_process | arabinan catabolic process |
B | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
B | 0046558 | molecular_function | arabinan endo-1,5-alpha-L-arabinosidase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:12198486 |
Chain | Residue | Details |
B | ASP38 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:12198486 |
Chain | Residue | Details |
B | GLU221 |
site_id | SWS_FT_FI3 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12198486 |
Chain | Residue | Details |
B | ASP35 | |
B | ASP90 | |
B | GLY115 | |
B | ASN155 | |
B | SER175 | |
B | GLU221 | |
B | GLN316 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
B | HIS291 |
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:12198486 |
Chain | Residue | Details |
B | ALA158 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Important for substrate recognition and stabilization |
Chain | Residue | Details |
B | HIS291 |