5HSJ
Structure of tyrosine decarboxylase complex with PLP at 1.9 Angstroms resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| A | 0004837 | molecular_function | tyrosine decarboxylase activity |
| 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 | 0036468 | molecular_function | L-dopa decarboxylase activity |
| B | 0004058 | molecular_function | aromatic-L-amino-acid decarboxylase activity |
| B | 0004837 | molecular_function | tyrosine decarboxylase activity |
| 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 | 0036468 | molecular_function | L-dopa decarboxylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue PLP A 701 |
| Chain | Residue |
| A | ASP157 |
| A | LYS392 |
| B | SER440 |
| A | GLY158 |
| A | SER159 |
| A | ASN162 |
| A | HIS241 |
| A | THR298 |
| A | ASP328 |
| A | ASP389 |
| A | HIS391 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide PLP B 702 and LYS B 392 |
| Chain | Residue |
| A | GLY439 |
| A | SER440 |
| B | ASP157 |
| B | GLY158 |
| B | SER159 |
| B | ASN162 |
| B | HIS241 |
| B | THR298 |
| B | ASP328 |
| B | ASP389 |
| B | PRO390 |
| B | HIS391 |
| B | MET393 |
| B | GLY394 |
| B | TYR395 |
| B | HOH848 |
| B | HOH1090 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:27292129 |
| Chain | Residue | Details |
| A | TYR420 | |
| B | TYR420 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:27292129 |
| Chain | Residue | Details |
| A | ASP389 | |
| B | GLY158 | |
| B | THR298 | |
| B | ASP389 | |
| A | GLY158 | |
| A | THR298 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27292129 |
| Chain | Residue | Details |
| A | SER440 | |
| B | SER440 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:27292129, ECO:0007744|PDB:5HSJ |
| Chain | Residue | Details |
| A | LYS392 | |
| B | LYS392 |
