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 | 6 |
| Details | BINDING SITE FOR RESIDUE K A 500 |
| Chain | Residue |
| A | GLY52 |
| A | ASN262 |
| A | HOH510 |
| B | GLU69 |
| B | HOH501 |
| B | HOH535 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 500 |
| Chain | Residue |
| B | ASN262 |
| B | HOH516 |
| B | HOH519 |
| A | GLU69 |
| A | HOH504 |
| B | GLY52 |
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 | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
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 | LLP257 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | SER385 | electrostatic stabiliser |
| A | ARG452 | 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 | LLP257 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | SER385 | electrostatic stabiliser |
| B | ARG452 | electrostatic stabiliser, ground state destabiliser |
