1T6J
Crystal Structure of Phenylalanine Ammonia Lyase from Rhodosporidium toruloides
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 | 0016829 | molecular_function | lyase activity |
A | 0016841 | molecular_function | ammonia-lyase activity |
A | 0045548 | molecular_function | phenylalanine ammonia-lyase activity |
A | 0052883 | molecular_function | tyrosine 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 | 0016829 | molecular_function | lyase activity |
B | 0016841 | molecular_function | ammonia-lyase activity |
B | 0045548 | molecular_function | phenylalanine ammonia-lyase activity |
B | 0052883 | molecular_function | tyrosine ammonia-lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CIN B 1001 |
Chain | Residue |
B | 175211 |
B | LEU266 |
B | ASN397 |
B | LYS468 |
B | GLU496 |
B | GLN500 |
Functional Information from PROSITE/UniProt
site_id | PS00488 |
Number of Residues | 17 |
Details | PAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GTISASGDLsPLSyiaA |
Chain | Residue | Details |
A | GLY207-ILE225 |
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 | THR272 | |
B | ALA501 | |
A | ARG362 | |
A | SER368 | |
A | LEU399 | |
A | ALA501 | |
B | THR272 | |
B | ARG362 | |
B | SER368 | |
B | LEU399 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15350127, ECO:0007744|PDB:1T6J |
Chain | Residue | Details |
A | LEU470 | |
A | ALA498 | |
B | LEU470 | |
B | ALA498 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: 2,3-didehydroalanine (Ser) => ECO:0000269|PubMed:15350127 |
Chain | Residue | Details |
A | ASP214 | |
B | ASP214 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CROSSLNK: 5-imidazolinone (Ala-Gly) => ECO:0000269|PubMed:15350127 |
Chain | Residue | Details |
A | 175211 | |
A | LEU215 | |
B | 175211 | |
B | LEU215 |