5E2J
Crystal structure of single mutant thermostable endoglucanase (D468A) from Alicyclobacillus acidocaldarius
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008810 | molecular_function | cellulase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030245 | biological_process | cellulose catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008810 | molecular_function | cellulase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0030245 | biological_process | cellulose catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 601 |
| Chain | Residue |
| A | ASP302 |
| A | GLU304 |
| A | ASP307 |
| A | GLU308 |
| A | ALA344 |
| A | HOH807 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 602 |
| Chain | Residue |
| A | HIS142 |
| A | CYS104 |
| A | CYS121 |
| A | HIS122 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MPD A 603 |
| Chain | Residue |
| A | PRO33 |
| A | ALA35 |
| A | ARG37 |
| A | THR73 |
| B | MPD603 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MPD A 604 |
| Chain | Residue |
| A | TRP339 |
| A | GLU340 |
| A | GLU377 |
| A | LEU381 |
| A | ARG410 |
| A | ALA413 |
| A | HOH707 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 601 |
| Chain | Residue |
| B | ASP302 |
| B | GLU304 |
| B | ASP307 |
| B | GLU308 |
| B | ALA344 |
| B | HOH744 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 602 |
| Chain | Residue |
| B | CYS104 |
| B | CYS121 |
| B | HIS122 |
| B | HIS142 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 603 |
| Chain | Residue |
| A | ARG37 |
| A | MPD603 |
| B | ALA35 |
| B | THR73 |
| B | HOH734 |
Functional Information from PROSITE/UniProt
| site_id | PS00592 |
| Number of Residues | 27 |
| Details | GH9_2 Glycosyl hydrolases family 9 (GH9) active site signature 2. YLFGaNplgqCYVTGf....GqrPVrhPHHR |
| Chain | Residue | Details |
| A | TYR437-ARG463 |
| site_id | PS00698 |
| Number of Residues | 19 |
| Details | GH9_3 Glycosyl hydrolases family 9 (GH9) active site signature 3. YiDhqdsYstnEvAvywNS |
| Chain | Residue | Details |
| A | TYR504-SER522 |
