3KDZ
X-ray crystal structure of a tyrosine aminomutase mutant construct with bound ligand
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004397 | molecular_function | histidine ammonia-lyase activity |
| A | 0006548 | biological_process | L-histidine catabolic process |
| A | 0009403 | biological_process | toxin biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016841 | molecular_function | ammonia-lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0050368 | molecular_function | L-tyrosine 2,3-aminomutase activity |
| A | 0052883 | molecular_function | tyrosine ammonia-lyase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004397 | molecular_function | histidine ammonia-lyase activity |
| B | 0006548 | biological_process | L-histidine catabolic process |
| B | 0009403 | biological_process | toxin biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016841 | molecular_function | ammonia-lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0050368 | molecular_function | L-tyrosine 2,3-aminomutase activity |
| B | 0052883 | molecular_function | tyrosine ammonia-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TYR A 600 |
| Chain | Residue |
| A | PHE63 |
| A | GLN442 |
| A | HOH673 |
| B | TYR308 |
| B | ARG311 |
| A | TYR69 |
| A | HIS93 |
| A | MDO152 |
| A | ASN205 |
| A | ASN341 |
| A | PHE356 |
| A | TYR415 |
| A | ASN438 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE TYR B 600 |
| Chain | Residue |
| A | GLN305 |
| A | TYR308 |
| A | ARG311 |
| B | PHE63 |
| B | TYR69 |
| B | HIS93 |
| B | MDO152 |
| B | LEU156 |
| B | ASN205 |
| B | ASN341 |
| B | PHE356 |
| B | TYR415 |
| B | GLN442 |
| B | HOH690 |
| B | HOH692 |
Functional Information from PROSITE/UniProt
| site_id | PS00488 |
| Number of Residues | 17 |
| Details | PAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GSLGASGDLaPLShvaS |
| Chain | Residue | Details |
| A | GLY148-LEU166 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:18078753 |
| Chain | Residue | Details |
| A | PHE63 | |
| B | PHE63 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20577998 |
| Chain | Residue | Details |
| A | HIS93 | |
| A | THR207 | |
| A | ILE313 | |
| B | HIS93 | |
| B | THR207 | |
| B | ILE313 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: 2,3-didehydroalanine (Ser) => ECO:0000269|PubMed:17516659 |
| Chain | Residue | Details |
| A | ASP155 | |
| B | ASP155 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | CROSSLNK: 5-imidazolinone (Ala-Gly) => ECO:0000269|PubMed:17516659 |
| Chain | Residue | Details |
| A | MDO152 | |
| A | LEU156 | |
| B | MDO152 | |
| B | LEU156 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 245 |
| Chain | Residue | Details |
| A | PHE63 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY70 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 245 |
| Chain | Residue | Details |
| B | PHE63 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLY70 | electrostatic stabiliser, hydrogen bond donor |
