3IWR
Crystal structure of class I chitinase from Oryza sativa L. japonica
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0004568 | molecular_function | chitinase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006032 | biological_process | chitin catabolic process |
A | 0006952 | biological_process | defense response |
A | 0008061 | molecular_function | chitin binding |
A | 0008843 | molecular_function | endochitinase activity |
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 | 0050832 | biological_process | defense response to fungus |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0004568 | molecular_function | chitinase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006032 | biological_process | chitin catabolic process |
B | 0006952 | biological_process | defense response |
B | 0008061 | molecular_function | chitin binding |
B | 0008843 | molecular_function | endochitinase activity |
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 | 0050832 | biological_process | defense response to fungus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MES A 1 |
Chain | Residue |
A | GLU154 |
A | ILE204 |
A | GLN205 |
A | LEU206 |
A | SER207 |
A | ASN211 |
A | VAL285 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 341 |
Chain | Residue |
A | PRO276 |
A | ARG142 |
A | ILE259 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MES B 2 |
Chain | Residue |
B | GLU154 |
B | ILE204 |
B | GLN205 |
B | LEU206 |
B | SER207 |
B | ASN211 |
B | VAL285 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD B 341 |
Chain | Residue |
B | HOH9 |
B | THR139 |
B | ARG142 |
B | ILE259 |
Functional Information from PROSITE/UniProt
site_id | PS00026 |
Number of Residues | 20 |
Details | CHIT_BIND_I_1 Chitin recognition or binding domain signature. Cpncl.CCSrwGwCGttsdFC |
Chain | Residue | Details |
A | CYS44-CYS63 |
site_id | PS00773 |
Number of Residues | 23 |
Details | CHITINASE_19_1 Chitinases family 19 signature 1. Cparg.FYTyeaFLaAaaaFpaFG |
Chain | Residue | Details |
A | CYS110-GLY132 |
site_id | PS00774 |
Number of Residues | 11 |
Details | CHITINASE_19_2 Chitinases family 19 signature 2. VSFkTALWFWM |
Chain | Residue | Details |
A | VAL236-MET246 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P29022","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |