1WVU
Crystal structure of chitinase C from Streptomyces griseus HUT6037
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004568 | molecular_function | chitinase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006032 | biological_process | chitin catabolic process |
| A | 0006952 | biological_process | defense response |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0050832 | biological_process | defense response to fungus |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004568 | molecular_function | chitinase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006032 | biological_process | chitin catabolic process |
| B | 0006952 | biological_process | defense response |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016998 | biological_process | cell wall macromolecule catabolic process |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0050832 | biological_process | defense response to fungus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 295 |
| Chain | Residue |
| A | SER145 |
| A | HIS146 |
| A | LYS276 |
| B | GLN279 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 295 |
| Chain | Residue |
| B | ILE154 |
| B | LYS155 |
| B | HOH339 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 296 |
| Chain | Residue |
| B | TYR111 |
| B | HOH379 |
| B | ARG105 |
| B | THR110 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 296 |
| Chain | Residue |
| A | GLU159 |
| A | LYS222 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 297 |
| Chain | Residue |
| A | ASN275 |
| B | ASN104 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 298 |
| Chain | Residue |
| A | TYR121 |
| A | PRO122 |
| A | ALA123 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 299 |
| Chain | Residue |
| A | ARG105 |
| A | THR110 |
| A | TYR111 |
| A | HOH360 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 300 |
| Chain | Residue |
| A | LYS155 |
| A | ASP216 |
| A | PRO217 |
| A | ALA218 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 297 |
| Chain | Residue |
| B | THR287 |
| B | THR288 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 298 |
| Chain | Residue |
| B | GLN178 |
| B | GLY203 |
| B | HOH337 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 301 |
| Chain | Residue |
| A | GLN178 |
| A | GLY203 |
| A | HOH350 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | ASN266 |
| B | ASN266 |
| B | GLN269 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 299 |
| Chain | Residue |
| B | TYR121 |
| B | PRO122 |
| B | ALA123 |
| B | HOH318 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 819 |
| Chain | Residue | Details |
| A | GLU147 | promote heterolysis, proton acceptor, proton donor |
| A | GLU156 | activator, electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor |
| A | ASN194 | steric role |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 819 |
| Chain | Residue | Details |
| B | GLU147 | promote heterolysis, proton acceptor, proton donor |
| B | GLU156 | activator, electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor |
| B | ASN194 | steric role |
