6ZMV
Structure of muramidase from Trichobolus zukalii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| B | 0003796 | molecular_function | lysozyme activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0009253 | biological_process | peptidoglycan catabolic process |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0016998 | biological_process | cell wall macromolecule catabolic process |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0042742 | biological_process | defense response to bacterium |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | ASP6 |
| A | ILE7 |
| A | SER8 |
| A | GLN11 |
| A | TYR59 |
| A | ASP189 |
| A | HOH462 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | MET93 |
| A | ASP95 |
| A | GLU97 |
| A | TYR134 |
| A | GLN179 |
| A | ASP189 |
| A | HOH424 |
| A | ASP6 |
| A | TYR59 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | MET96 |
| A | TYR98 |
| A | TYR134 |
| A | THR135 |
| A | GLY136 |
| A | TRP139 |
| A | HOH428 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 304 |
| Chain | Residue |
| A | TYR46 |
| A | ARG56 |
| A | SER84 |
| A | ASP86 |
| A | THR89 |
| A | GLN109 |
| A | HOH405 |
| A | HOH547 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 305 |
| Chain | Residue |
| A | LYS124 |
| A | ARG129 |
| A | TYR130 |
| A | HOH402 |
| A | HOH409 |
| A | HOH435 |
| A | HOH437 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 301 |
| Chain | Residue |
| B | ASP6 |
| B | ILE7 |
| B | SER8 |
| B | GLN11 |
| B | TYR59 |
| B | ASP189 |
| B | HOH491 |
| B | HOH594 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| B | ASP6 |
| B | TYR59 |
| B | MET93 |
| B | ASP95 |
| B | GLU97 |
| B | TYR134 |
| B | GLN179 |
| B | ASP189 |
| B | HOH408 |
| B | HOH426 |
| B | HOH445 |
| B | HOH488 |
| B | HOH611 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | MET96 |
| B | GLU97 |
| B | TYR98 |
| B | TYR134 |
| B | THR135 |
| B | GLY136 |
| B | TRP139 |
| B | HOH422 |
| B | HOH468 |
| B | HOH577 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| B | TYR46 |
| B | ARG56 |
| B | SER84 |
| B | ASP86 |
| B | THR89 |
| B | HOH484 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 305 |
| Chain | Residue |
| B | LYS124 |
| B | ARG129 |
| B | TYR130 |
| B | HOH404 |
| B | HOH420 |
| B | HOH471 |
| B | HOH502 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 306 |
| Chain | Residue |
| B | ARG63 |
| B | PRO64 |
| B | ALA65 |
| B | SER66 |
| B | HIS105 |
| B | HOH415 |
| B | HOH610 |
Functional Information from PROSITE/UniProt
| site_id | PS00953 |
| Number of Residues | 34 |
| Details | GLYCOSYL_HYDROL_F25_1 Glycosyl hydrolases family 25 active site signature. DIshyQPsvnyagayns.....GarfvIIKaTEGttYtD |
| Chain | Residue | Details |
| A | ASP6-ASP39 |
