1JS6
Crystal Structure of DOPA decarboxylase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006584 | biological_process | catecholamine metabolic process |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0036467 | molecular_function | 5-hydroxy-L-tryptophan decarboxylase activity |
| A | 0036468 | molecular_function | L-dopa decarboxylase activity |
| A | 0042416 | biological_process | dopamine biosynthetic process |
| A | 0042423 | biological_process | catecholamine biosynthetic process |
| A | 0042427 | biological_process | serotonin biosynthetic process |
| B | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006584 | biological_process | catecholamine metabolic process |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0036467 | molecular_function | 5-hydroxy-L-tryptophan decarboxylase activity |
| B | 0036468 | molecular_function | L-dopa decarboxylase activity |
| B | 0042416 | biological_process | dopamine biosynthetic process |
| B | 0042423 | biological_process | catecholamine biosynthetic process |
| B | 0042427 | biological_process | serotonin biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 601 |
| Chain | Residue |
| A | PHE80 |
| A | HIS302 |
| A | LYS303 |
| A | HOH609 |
| B | HOH604 |
| A | SER147 |
| A | ALA148 |
| A | SER149 |
| A | HIS192 |
| A | THR246 |
| A | ASP271 |
| A | ALA273 |
| A | ASN300 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 602 |
| Chain | Residue |
| B | PHE80 |
| B | SER147 |
| B | ALA148 |
| B | SER149 |
| B | HIS192 |
| B | THR246 |
| B | ASP271 |
| B | ALA273 |
| B | ASN300 |
| B | HIS302 |
| B | LYS303 |
| B | HOH620 |
| B | HOH624 |
Functional Information from PROSITE/UniProt
| site_id | PS00392 |
| Number of Residues | 22 |
| Details | DDC_GAD_HDC_YDC DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site. SFnFnphKWLlVnFDCsaMWvK |
| Chain | Residue | Details |
| A | SER296-LYS317 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11685243, ECO:0007744|PDB:1JS3 |
| Chain | Residue | Details |
| A | THR82 | |
| A | HIS192 | |
| B | THR82 | |
| B | HIS192 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P20711 |
| Chain | Residue | Details |
| A | ALA148 | |
| A | THR246 | |
| A | ASN300 | |
| B | ALA148 | |
| B | SER149 | |
| B | THR246 | |
| B | ASN300 | |
| A | SER149 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:1935935 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11685243 |
| Chain | Residue | Details |
| A | LYS303 | |
| B | LYS303 |
