Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006570 | biological_process | tyrosine metabolic process |
| A | 0009072 | biological_process | aromatic amino acid metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0050371 | molecular_function | tyrosine phenol-lyase activity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006570 | biological_process | tyrosine metabolic process |
| B | 0009072 | biological_process | aromatic amino acid metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0050371 | molecular_function | tyrosine phenol-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PM9 A 1457 |
| Chain | Residue |
| A | THR49 |
| A | ASP214 |
| A | THR216 |
| A | ARG217 |
| A | SER254 |
| A | LYS257 |
| A | MET379 |
| A | ARG381 |
| A | ARG404 |
| A | PHE449 |
| A | HOH2425 |
| A | GLN98 |
| B | TYR71 |
| A | GLY99 |
| A | ARG100 |
| A | GLU103 |
| A | PHE123 |
| A | THR124 |
| A | THR125 |
| A | ASN185 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 1458 |
| Chain | Residue |
| A | GLY52 |
| A | ASN262 |
| A | HOH2083 |
| B | GLU69 |
| B | HOH2311 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 1257 |
| Chain | Residue |
| B | GLN98 |
| B | GLY99 |
| B | ARG100 |
| B | GLU103 |
| B | PHE123 |
| B | THR126 |
| B | ASN185 |
| B | ASP214 |
| B | THR216 |
| B | ARG217 |
| B | SER254 |
| B | LYS257 |
| B | HOH2223 |
| B | HOH2458 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 1458 |
| Chain | Residue |
| A | GLU69 |
| A | HOH2100 |
| A | HOH2299 |
| B | GLY52 |
| B | ASN262 |
| B | HOH2289 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGE A 1459 |
| Chain | Residue |
| A | LYS226 |
| A | GLU233 |
| A | TYR312 |
| A | HOH2426 |
| A | HOH2427 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE P33 A 1460 |
| Chain | Residue |
| A | MET1 |
| A | TYR3 |
| A | ASP418 |
| A | HOH2429 |
| B | TYR3 |
| B | TYR324 |
| B | TYR414 |
| B | ALA415 |
| B | ASP418 |
| B | VAL419 |
| B | ASP422 |
| B | HOH2415 |
Functional Information from PROSITE/UniProt
| site_id | PS00853 |
| Number of Residues | 19 |
| Details | BETA_ELIM_LYASE Beta-eliminating lyases pyridoxal-phosphate attachment site. YaDgctMSGKKDcLVnIGG |
| Chain | Residue | Details |
| A | TYR247-GLY265 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LYS257 | |
| B | LYS257 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | PHE123 | |
| A | ASP214 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | PHE123 | |
| B | ASP214 | |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | TYR71 | |
| A | ARG381 | |
| A | PHE123 | |
| A | ASP214 | |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | TYR71 | |
| B | ARG381 | |
| B | PHE123 | |
| B | ASP214 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | ASP214 | |
| A | LYS256 | |
| A | TYR128 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | ASP214 | |
| B | LYS256 | |
| B | TYR128 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 933 |
| Chain | Residue | Details |
| A | TYR71 | proton acceptor, proton donor |
| A | PHE123 | steric role |
| A | THR124 | electrostatic stabiliser |
| A | ASP214 | electrostatic stabiliser |
| A | LYS257 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ARG381 | electrostatic stabiliser |
| A | PHE448 | electrostatic stabiliser, ground state destabiliser |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 933 |
| Chain | Residue | Details |
| B | TYR71 | proton acceptor, proton donor |
| B | PHE123 | steric role |
| B | THR124 | electrostatic stabiliser |
| B | ASP214 | electrostatic stabiliser |
| B | LYS257 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ARG381 | electrostatic stabiliser |
| B | PHE448 | electrostatic stabiliser, ground state destabiliser |
