1LL6
STRUCTURE OF THE D169N MUTANT OF C. IMMITIS CHITINASE 1
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 | 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 | 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 |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| 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 | 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 |
| C | 0000272 | biological_process | polysaccharide catabolic process |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0004568 | molecular_function | chitinase activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006032 | biological_process | chitin catabolic process |
| C | 0008061 | molecular_function | chitin binding |
| C | 0008843 | molecular_function | endochitinase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0000272 | biological_process | polysaccharide catabolic process |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0004568 | molecular_function | chitinase activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0006032 | biological_process | chitin catabolic process |
| D | 0008061 | molecular_function | chitin binding |
| D | 0008843 | molecular_function | endochitinase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PROSITE/UniProt
| site_id | PS01095 |
| Number of Residues | 9 |
| Details | GH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGIDINwE |
| Chain | Residue | Details |
| A | PHE163-GLU171 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1452 |
| Details | Domain: {"description":"GH18","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| A | ASN169 | |
| A | TYR239 | |
| A | GLU171 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| B | ASP167 | |
| B | GLU171 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| C | ASP167 | |
| C | GLU171 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| D | ASP167 | |
| D | GLU171 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| B | ASN169 | |
| B | TYR239 | |
| B | GLU171 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| C | ASN169 | |
| C | TYR239 | |
| C | GLU171 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| D | ASN169 | |
| D | TYR239 | |
| D | GLU171 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| A | ASN169 | |
| A | GLU171 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| B | ASN169 | |
| B | GLU171 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| C | ASN169 | |
| C | GLU171 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| D | ASN169 | |
| D | GLU171 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ctn |
| Chain | Residue | Details |
| A | ASP167 | |
| A | GLU171 |
