1W27
Phenylalanine ammonia-lyase (PAL) from Petroselinum crispum
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006559 | biological_process | L-phenylalanine catabolic process |
A | 0009698 | biological_process | phenylpropanoid metabolic process |
A | 0009800 | biological_process | cinnamic acid biosynthetic process |
A | 0016597 | molecular_function | amino acid binding |
A | 0016829 | molecular_function | lyase activity |
A | 0016841 | molecular_function | ammonia-lyase activity |
A | 0032991 | cellular_component | protein-containing complex |
A | 0045548 | molecular_function | phenylalanine ammonia-lyase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006559 | biological_process | L-phenylalanine catabolic process |
B | 0009698 | biological_process | phenylpropanoid metabolic process |
B | 0009800 | biological_process | cinnamic acid biosynthetic process |
B | 0016597 | molecular_function | amino acid binding |
B | 0016829 | molecular_function | lyase activity |
B | 0016841 | molecular_function | ammonia-lyase activity |
B | 0032991 | cellular_component | protein-containing complex |
B | 0045548 | molecular_function | phenylalanine ammonia-lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DTT A 1717 |
Chain | Residue |
A | PHE137 |
A | MDO203 |
A | LEU206 |
A | ASN260 |
A | HOH2240 |
A | HOH2386 |
A | HOH2533 |
A | HOH2534 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DTT B 1717 |
Chain | Residue |
B | MDO203 |
B | LEU206 |
B | ASN260 |
B | HOH2392 |
B | HOH2400 |
B | HOH2537 |
B | PHE137 |
Functional Information from PROSITE/UniProt
site_id | PS00488 |
Number of Residues | 17 |
Details | PAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GTITASGDLvPLSyiaG |
Chain | Residue | Details |
A | GLY198-LEU216 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q68G84 |
Chain | Residue | Details |
A | TYR110 | |
B | TYR110 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q68G84 |
Chain | Residue | Details |
A | ASN260 | |
B | ASN487 | |
A | GLN348 | |
A | ARG354 | |
A | ASN384 | |
A | ASN487 | |
B | ASN260 | |
B | GLN348 | |
B | ARG354 | |
B | ASN384 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P11544 |
Chain | Residue | Details |
A | LYS456 | |
A | GLU484 | |
B | LYS456 | |
B | GLU484 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: 2,3-didehydroalanine (Ser) => ECO:0000269|PubMed:8050576 |
Chain | Residue | Details |
A | ASP205 | |
B | ASP205 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CROSSLNK: 5-imidazolinone (Ala-Gly) => ECO:0000250|UniProtKB:Q68G84 |
Chain | Residue | Details |
A | MDO203 | |
A | LEU206 | |
B | MDO203 | |
B | LEU206 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 15548745 |
Chain | Residue | Details |
A | PHE400 | |
B | TYR351 |
site_id | CSA2 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 15548745 |
Chain | Residue | Details |
B | PHE400 |
site_id | CSA3 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 15548745 |
Chain | Residue | Details |
A | PHE400 | |
B | TYR351 |
site_id | CSA4 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 15548745 |
Chain | Residue | Details |
A | TYR351 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 708 |
Chain | Residue | Details |
A | TYR110 | increase acidity, promote heterolysis, proton donor |
A | TYR351 | proton acceptor, proton donor, proton relay |
A | PHE400 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 708 |
Chain | Residue | Details |
B | TYR110 | increase acidity, promote heterolysis, proton donor |
B | TYR351 | proton acceptor, proton donor, proton relay |
B | PHE400 | electrostatic stabiliser |