6ZE8
Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008061 | molecular_function | chitin binding |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008061 | molecular_function | chitin binding |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0008061 | molecular_function | chitin binding |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0008061 | molecular_function | chitin binding |
| E | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| E | 0005975 | biological_process | carbohydrate metabolic process |
| E | 0008061 | molecular_function | chitin binding |
| F | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| F | 0005975 | biological_process | carbohydrate metabolic process |
| F | 0008061 | molecular_function | chitin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue QGB A 401 |
| Chain | Residue |
| A | TYR27 |
| A | THR295 |
| A | GLU297 |
| A | MET300 |
| A | MET356 |
| A | TRP358 |
| A | HOH516 |
| A | HOH715 |
| A | TRP99 |
| A | ASP138 |
| A | GLU140 |
| A | ALA183 |
| A | MET210 |
| A | TYR212 |
| A | ASP213 |
| A | TYR267 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 402 |
| Chain | Residue |
| A | GLY187 |
| A | TYR190 |
| A | HOH651 |
| A | HOH761 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue QGB B 401 |
| Chain | Residue |
| B | TYR27 |
| B | TRP99 |
| B | ASP138 |
| B | GLU140 |
| B | ALA183 |
| B | MET210 |
| B | TYR212 |
| B | ASP213 |
| B | TYR267 |
| B | THR295 |
| B | GLU297 |
| B | MET300 |
| B | MET356 |
| B | TRP358 |
| B | HOH676 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue NA B 402 |
| Chain | Residue |
| B | ASN100 |
| B | HOH871 |
| B | HOH873 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | binding site for residue QGB C 401 |
| Chain | Residue |
| C | TYR27 |
| C | TRP99 |
| C | ASP138 |
| C | GLU140 |
| C | ALA183 |
| C | MET210 |
| C | TYR212 |
| C | ASP213 |
| C | TYR267 |
| C | THR295 |
| C | GLU297 |
| C | MET300 |
| C | MET356 |
| C | TRP358 |
| C | LEU362 |
| C | HOH501 |
| C | HOH507 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue NA C 402 |
| Chain | Residue |
| C | ALA149 |
| C | VAL150 |
| C | LYS152 |
| C | GLU153 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | binding site for residue QGB D 401 |
| Chain | Residue |
| D | TYR27 |
| D | TRP99 |
| D | ASP138 |
| D | GLU140 |
| D | ALA183 |
| D | MET210 |
| D | TYR212 |
| D | ASP213 |
| D | TYR267 |
| D | THR295 |
| D | GLU297 |
| D | MET300 |
| D | MET356 |
| D | TRP358 |
| D | LEU362 |
| D | HOH659 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 402 |
| Chain | Residue |
| C | ARG125 |
| C | HOH820 |
| C | HOH847 |
| D | LYS321 |
| D | HOH628 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue NA D 403 |
| Chain | Residue |
| D | LYS314 |
| D | PHE334 |
| D | HOH828 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for residue QGB E 401 |
| Chain | Residue |
| E | TYR27 |
| E | TRP99 |
| E | ASP138 |
| E | GLU140 |
| E | ALA183 |
| E | MET210 |
| E | TYR212 |
| E | ASP213 |
| E | TYR267 |
| E | THR295 |
| E | GLU297 |
| E | MET300 |
| E | MET356 |
| E | TRP358 |
| E | HOH505 |
| E | HOH771 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue NA E 402 |
| Chain | Residue |
| E | GLU74 |
| E | GLN78 |
| site_id | AD3 |
| Number of Residues | 16 |
| Details | binding site for residue QGB F 401 |
| Chain | Residue |
| F | TYR27 |
| F | TRP99 |
| F | ASP138 |
| F | GLU140 |
| F | ALA183 |
| F | MET210 |
| F | TYR212 |
| F | ASP213 |
| F | TYR267 |
| F | THR295 |
| F | GLU297 |
| F | MET300 |
| F | MET356 |
| F | TRP358 |
| F | HOH504 |
| F | HOH509 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue NA F 402 |
| Chain | Residue |
| D | HOH863 |
| F | LYS44 |
| F | HOH845 |
| F | HOH858 |
Functional Information from PROSITE/UniProt
| site_id | PS01095 |
| Number of Residues | 9 |
| Details | GH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGLDLDwE |
| Chain | Residue | Details |
| A | PHE132-GLU140 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258 |
| Chain | Residue | Details |
| A | GLU140 | |
| B | GLU140 | |
| C | GLU140 | |
| D | GLU140 | |
| E | GLU140 | |
| F | GLU140 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 |
| Chain | Residue | Details |
| A | GLU70 | |
| B | TRP358 | |
| C | GLU70 | |
| C | GLY97 | |
| C | TYR141 | |
| C | MET210 | |
| C | TRP358 | |
| D | GLU70 | |
| D | GLY97 | |
| D | TYR141 | |
| D | MET210 | |
| A | GLY97 | |
| D | TRP358 | |
| E | GLU70 | |
| E | GLY97 | |
| E | TYR141 | |
| E | MET210 | |
| E | TRP358 | |
| F | GLU70 | |
| F | GLY97 | |
| F | TYR141 | |
| F | MET210 | |
| A | TYR141 | |
| F | TRP358 | |
| A | MET210 | |
| A | TRP358 | |
| B | GLU70 | |
| B | GLY97 | |
| B | TYR141 | |
| B | MET210 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; in variant S-102 => ECO:0000269|PubMed:19725875 |
| Chain | Residue | Details |
| A | ASN100 | |
| B | ASN100 | |
| C | ASN100 | |
| D | ASN100 | |
| E | ASN100 | |
| F | ASN100 |
