3TE4
Crystal structure of dopamine N Acetyltransferase in complex with acetyl-COA from Drosophila Melanogaster
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE ACO A 231 |
| Chain | Residue |
| A | PHE43 |
| A | LEU146 |
| A | SER147 |
| A | VAL148 |
| A | ARG153 |
| A | GLY154 |
| A | LEU155 |
| A | GLY156 |
| A | ILE157 |
| A | ALA158 |
| A | LEU180 |
| A | ASP46 |
| A | SER182 |
| A | LYS192 |
| A | HOH236 |
| A | HOH240 |
| A | HOH246 |
| A | HOH251 |
| A | HOH252 |
| A | HOH262 |
| A | HOH263 |
| A | HOH265 |
| A | PRO48 |
| A | HOH281 |
| A | HOH293 |
| A | HOH295 |
| A | HOH319 |
| A | HOH380 |
| A | HOH394 |
| A | HOH402 |
| A | HOH456 |
| A | HOH459 |
| A | HOH565 |
| A | ASP132 |
| A | HOH571 |
| A | VAL133 |
| A | PRO135 |
| A | GLY143 |
| A | LYS144 |
| A | ILE145 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22716280, ECO:0007744|PDB:3TE4 |
| Chain | Residue | Details |
| A | CYS181 | |
| A | VAL189 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | SITE: Has a role in the catalytic activity => ECO:0000269|PubMed:25406072 |
| Chain | Residue | Details |
| A | GLY82 | |
| A | ALA217 | |
| A | VAL221 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Might be involved in substrate binding => ECO:0000269|PubMed:25406072 |
| Chain | Residue | Details |
| A | ASP99 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | SITE: Regulates binding affinity for coenzyme A (CoASH) => ECO:0000269|PubMed:25406072 |
| Chain | Residue | Details |
| A | ARG188 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Acetyl-CoA => ECO:0000269|PubMed:22716280, ECO:0007744|PDB:3TE4 |
| Chain | Residue | Details |
| A | ALA227 |
