6B6L
The crystal structure of glycosyl hydrolase family 2 (GH2) member from Bacteroides cellulosilyticus DSM 14838
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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 801 |
| Chain | Residue |
| A | TYR136 |
| A | PHE381 |
| A | LEU400 |
| A | ASP404 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 802 |
| Chain | Residue |
| A | GLU573 |
| A | ALA349 |
| A | PHE351 |
| A | ASP558 |
| A | ARG565 |
| A | SER569 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue FMT A 803 |
| Chain | Residue |
| A | ASN167 |
| A | CYS168 |
| A | ARG169 |
| A | TRP170 |
| A | THR172 |
| A | HOH1102 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue FMT A 804 |
| Chain | Residue |
| A | GLU515 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 801 |
| Chain | Residue |
| B | ALA349 |
| B | PHE351 |
| B | ASP558 |
| B | ARG565 |
| B | SER569 |
| B | ARG572 |
| B | GLU573 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue FMT B 802 |
| Chain | Residue |
| B | ILE296 |
| B | GLY297 |
| B | ASN414 |
| B | PRO416 |
| B | HOH1004 |
Functional Information from PROSITE/UniProt
| site_id | PS00608 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DRNHPSVIMWSig.NE |
| Chain | Residue | Details |
| A | ASP412-GLU426 |
