6EEM
Crystal structure of Papaver somniferum tyrosine decarboxylase in complex with L-tyrosine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004837 | molecular_function | tyrosine decarboxylase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006520 | biological_process | amino acid 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 |
B | 0004837 | molecular_function | tyrosine decarboxylase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006520 | biological_process | amino acid 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | binding site for residue 0PR A 601 |
Chain | Residue |
A | TRP90 |
A | ASP289 |
A | ALA291 |
A | ASN318 |
A | HIS320 |
A | LYS321 |
A | LEU327 |
A | HOH717 |
B | VAL120 |
B | PHE122 |
B | TYR350 |
A | PHE99 |
B | LEU371 |
B | SER372 |
A | PRO100 |
A | THR168 |
A | THR169 |
A | CYS170 |
A | HIS205 |
A | THR260 |
A | THR264 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 602 |
Chain | Residue |
A | GLY189 |
A | ARG190 |
A | HOH764 |
B | ASN218 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 603 |
Chain | Residue |
A | ARG393 |
A | HOH773 |
B | LYS149 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 604 |
Chain | Residue |
A | PHE395 |
A | HIS399 |
A | THR488 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 605 |
Chain | Residue |
A | LYS183 |
A | GLY283 |
A | ILE284 |
A | ASP313 |
A | HOH787 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue TYR B 601 |
Chain | Residue |
A | TYR350 |
A | LEU371 |
A | SER372 |
B | TRP90 |
B | TYR98 |
B | PHE99 |
B | PRO100 |
B | SER101 |
B | HIS205 |
B | THR264 |
B | HIS320 |
B | LLP321 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 602 |
Chain | Residue |
A | ASN218 |
A | LYS220 |
B | GLY189 |
B | ARG190 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 603 |
Chain | Residue |
A | HIS304 |
B | PRO300 |
B | ARG393 |
B | ARG397 |
B | HOH708 |
B | HOH778 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 604 |
Chain | Residue |
A | PRO19 |
B | PHE395 |
B | HIS399 |
B | ALA487 |
B | THR488 |
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. SFsLnahKWFfTtLDCccLWvK |
Chain | Residue | Details |
B | SER314-LYS335 | |
A | SER314-LYS335 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:32371491, ECO:0007744|PDB:6EEM |
Chain | Residue | Details |
B | PRO100 | |
B | HIS205 | |
B | HIS320 | |
B | TYR350 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:32371491 |
Chain | Residue | Details |
B | LLP321 |