5E2J
Crystal structure of single mutant thermostable endoglucanase (D468A) from Alicyclobacillus acidocaldarius
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008810 | molecular_function | cellulase 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 | 0003824 | molecular_function | catalytic activity |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008810 | molecular_function | cellulase 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 |