1V8Z
X-ray crystal structure of the Tryptophan Synthase b2 Subunit from Hyperthermophile, Pyrococcus furiosus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | tryptophan biosynthetic process |
| A | 0004834 | molecular_function | tryptophan synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006568 | biological_process | tryptophan metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| B | 0000162 | biological_process | tryptophan biosynthetic process |
| B | 0004834 | molecular_function | tryptophan synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006568 | biological_process | tryptophan metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| C | 0000162 | biological_process | tryptophan biosynthetic process |
| C | 0004834 | molecular_function | tryptophan synthase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006568 | biological_process | tryptophan metabolic process |
| C | 0016829 | molecular_function | lyase activity |
| D | 0000162 | biological_process | tryptophan biosynthetic process |
| D | 0004834 | molecular_function | tryptophan synthase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006568 | biological_process | tryptophan metabolic process |
| D | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 389 |
| Chain | Residue |
| C | GLY227 |
| C | TYR301 |
| C | GLY303 |
| C | HOH405 |
| C | HOH419 |
| C | HOH461 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 389 |
| Chain | Residue |
| B | HOH404 |
| B | HOH474 |
| B | HOH483 |
| B | GLY227 |
| B | TYR301 |
| B | GLY303 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 389 |
| Chain | Residue |
| A | GLY227 |
| A | TYR301 |
| A | GLY303 |
| A | HOH410 |
| A | HOH454 |
| A | HOH455 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 400 |
| Chain | Residue |
| A | HIS81 |
| A | LYS82 |
| A | GLN109 |
| A | SER185 |
| A | CYS225 |
| A | GLY227 |
| A | GLY228 |
| A | GLY229 |
| A | SER230 |
| A | ASN231 |
| A | GLY298 |
| A | GLU345 |
| A | SER371 |
| A | GLY372 |
| A | HOH401 |
| A | HOH419 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP B 400 |
| Chain | Residue |
| B | HIS81 |
| B | LYS82 |
| B | GLN109 |
| B | SER185 |
| B | CYS225 |
| B | GLY227 |
| B | GLY228 |
| B | GLY229 |
| B | SER230 |
| B | ASN231 |
| B | GLU345 |
| B | SER371 |
| B | GLY372 |
| B | HOH402 |
| B | HOH411 |
| B | HOH436 |
| B | HOH467 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP C 400 |
| Chain | Residue |
| C | HIS81 |
| C | LYS82 |
| C | GLN109 |
| C | SER185 |
| C | CYS225 |
| C | GLY227 |
| C | GLY228 |
| C | GLY229 |
| C | SER230 |
| C | ASN231 |
| C | GLY298 |
| C | GLU345 |
| C | SER371 |
| C | GLY372 |
| C | HOH401 |
| C | HOH416 |
| C | HOH422 |
| C | HOH438 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP D 400 |
| Chain | Residue |
| D | HIS81 |
| D | LYS82 |
| D | GLN109 |
| D | SER185 |
| D | CYS225 |
| D | GLY227 |
| D | GLY228 |
| D | GLY229 |
| D | SER230 |
| D | ASN231 |
| D | GLY298 |
| D | GLU345 |
| D | SER371 |
| D | GLY372 |
| D | HOH402 |
| D | HOH413 |
Functional Information from PROSITE/UniProt
| site_id | PS00168 |
| Number of Residues | 15 |
| Details | TRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LvHgGAHKtNnaIgQ |
| Chain | Residue | Details |
| A | LEU75-GLN89 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS82 | |
| B | LYS82 | |
| C | LYS82 | |
| D | LYS82 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| A | HIS81 | |
| A | ASP300 | |
| A | LYS82 | |
| A | LYS162 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| B | HIS81 | |
| B | ASP300 | |
| B | LYS82 | |
| B | LYS162 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| C | HIS81 | |
| C | ASP300 | |
| C | LYS82 | |
| C | LYS162 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| D | HIS81 | |
| D | ASP300 | |
| D | LYS82 | |
| D | LYS162 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| A | LYS82 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| B | LYS82 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| C | LYS82 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| D | LYS82 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| A | LYS82 | |
| A | SER371 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| B | LYS82 | |
| B | SER371 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| C | LYS82 | |
| C | SER371 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| D | LYS82 | |
| D | SER371 |
