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 | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LLP257 | |
B | LLP257 | |
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 | 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 | LLP257 | 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 |