5M8E
Crystal structure of a GH43 arabonofuranosidase from Weissella sp. strain 142
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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CA A 401 |
Chain | Residue |
A | GLU76 |
A | HIS264 |
A | HOH503 |
A | HOH573 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue IMD A 402 |
Chain | Residue |
A | THR94 |
A | PHE96 |
A | PHE102 |
A | ASP291 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | TRP73 |
A | ARG298 |
A | GOL404 |
A | HOH628 |
A | ASP15 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | PHE136 |
A | LEU138 |
A | ASN163 |
A | GLU200 |
A | GOL403 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CA B 401 |
Chain | Residue |
B | GLU76 |
B | HIS264 |
B | HOH511 |
B | HOH659 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue IMD B 402 |
Chain | Residue |
B | THR94 |
B | PHE96 |
B | PHE102 |
B | ASP291 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | ASP15 |
B | TRP73 |
B | ARG298 |
B | HOH523 |