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 | 5 |
Details | binding site for residue CQG A 601 |
Chain | Residue |
A | PHE123 |
A | THR124 |
A | ARG381 |
A | PHE449 |
B | TYR71 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue K A 602 |
Chain | Residue |
B | ASN262 |
B | HOH1775 |
A | GLU69 |
A | HOH750 |
A | HOH761 |
B | GLY52 |
site_id | AC3 |
Number of Residues | 15 |
Details | binding site for residue 0JO A 603 |
Chain | Residue |
A | THR49 |
A | SER51 |
A | GLN98 |
A | GLY99 |
A | ARG100 |
A | GLU103 |
A | PHE123 |
A | ASN185 |
A | ASP214 |
A | ARG217 |
A | SER254 |
A | LYS257 |
A | ARG404 |
A | HOH709 |
B | TYR71 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue K A 604 |
Chain | Residue |
A | GLY52 |
A | ASN262 |
A | HOH756 |
A | HOH774 |
B | GLU69 |
B | HOH1729 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue P33 B 1601 |
Chain | Residue |
A | TYR3 |
A | TYR414 |
B | TYR3 |
B | TYR324 |
B | ASP418 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue CQG B 1602 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue CQG B 1603 |
site_id | AC8 |
Number of Residues | 15 |
Details | binding site for residue 0JO B 1604 |
Chain | Residue |
A | TYR71 |
B | THR49 |
B | GLN98 |
B | GLY99 |
B | ARG100 |
B | GLU103 |
B | PHE123 |
B | ASN185 |
B | ASP214 |
B | THR216 |
B | ARG217 |
B | SER254 |
B | LYS257 |
B | ARG404 |
B | HOH1704 |
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 | 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 | ALA448 | 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 | ALA448 | electrostatic stabiliser, ground state destabiliser |