1WDW
Structural basis of mutual activation of the tryptophan synthase a2b2 complex from a 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 | 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 | 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 | 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 | 0006568 | biological_process | tryptophan metabolic process |
| D | 0016829 | molecular_function | lyase activity |
| E | 0000162 | biological_process | tryptophan biosynthetic process |
| E | 0004834 | molecular_function | tryptophan synthase activity |
| E | 0006568 | biological_process | tryptophan metabolic process |
| E | 0016829 | molecular_function | lyase activity |
| F | 0000162 | biological_process | tryptophan biosynthetic process |
| F | 0004834 | molecular_function | tryptophan synthase activity |
| F | 0006568 | biological_process | tryptophan metabolic process |
| F | 0016829 | molecular_function | lyase activity |
| G | 0000162 | biological_process | tryptophan biosynthetic process |
| G | 0004834 | molecular_function | tryptophan synthase activity |
| G | 0006568 | biological_process | tryptophan metabolic process |
| G | 0016829 | molecular_function | lyase activity |
| H | 0000162 | biological_process | tryptophan biosynthetic process |
| H | 0004834 | molecular_function | tryptophan synthase activity |
| H | 0006568 | biological_process | tryptophan metabolic process |
| H | 0016829 | molecular_function | lyase activity |
| I | 0000162 | biological_process | tryptophan biosynthetic process |
| I | 0004834 | molecular_function | tryptophan synthase activity |
| I | 0006568 | biological_process | tryptophan metabolic process |
| I | 0016829 | molecular_function | lyase activity |
| J | 0000162 | biological_process | tryptophan biosynthetic process |
| J | 0004834 | molecular_function | tryptophan synthase activity |
| J | 0006568 | biological_process | tryptophan metabolic process |
| J | 0016829 | molecular_function | lyase activity |
| K | 0000162 | biological_process | tryptophan biosynthetic process |
| K | 0004834 | molecular_function | tryptophan synthase activity |
| K | 0006568 | biological_process | tryptophan metabolic process |
| K | 0016829 | molecular_function | lyase activity |
| L | 0000162 | biological_process | tryptophan biosynthetic process |
| L | 0004834 | molecular_function | tryptophan synthase activity |
| L | 0006568 | biological_process | tryptophan metabolic process |
| L | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 400 |
| Chain | Residue |
| B | HIS81 |
| B | GLY298 |
| B | GLU345 |
| B | SER371 |
| B | GLY372 |
| B | HOH412 |
| B | LYS82 |
| B | GLN109 |
| B | SER185 |
| B | GLY227 |
| B | GLY228 |
| B | GLY229 |
| B | SER230 |
| B | ASN231 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP D 400 |
| Chain | Residue |
| D | HIS81 |
| D | LYS82 |
| D | GLN109 |
| D | SER185 |
| D | GLY227 |
| D | GLY228 |
| D | GLY229 |
| D | SER230 |
| D | ASN231 |
| D | GLY298 |
| D | GLU345 |
| D | SER371 |
| D | GLY372 |
| D | HOH423 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP F 400 |
| Chain | Residue |
| F | HIS81 |
| F | LYS82 |
| F | GLN109 |
| F | SER185 |
| F | GLY227 |
| F | GLY228 |
| F | GLY229 |
| F | SER230 |
| F | ASN231 |
| F | GLY298 |
| F | GLU345 |
| F | SER371 |
| F | GLY372 |
| F | HOH433 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP H 400 |
| Chain | Residue |
| H | HIS81 |
| H | LYS82 |
| H | GLN109 |
| H | SER185 |
| H | GLY227 |
| H | GLY228 |
| H | GLY229 |
| H | SER230 |
| H | ASN231 |
| H | GLY298 |
| H | GLU345 |
| H | SER371 |
| H | GLY372 |
| H | HOH429 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP J 400 |
| Chain | Residue |
| J | HIS81 |
| J | LYS82 |
| J | GLN109 |
| J | SER185 |
| J | GLY227 |
| J | GLY228 |
| J | GLY229 |
| J | SER230 |
| J | ASN231 |
| J | GLY298 |
| J | GLU345 |
| J | SER371 |
| J | GLY372 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP L 400 |
| Chain | Residue |
| L | HIS81 |
| L | LYS82 |
| L | GLN109 |
| L | SER185 |
| L | GLY227 |
| L | GLY228 |
| L | GLY229 |
| L | SER230 |
| L | ASN231 |
| L | GLY298 |
| L | GLU345 |
| L | SER371 |
| L | GLY372 |
| L | HOH429 |
Functional Information from PROSITE/UniProt
| site_id | PS00167 |
| Number of Residues | 14 |
| Details | TRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. IELGiPFSDPIADG |
| Chain | Residue | Details |
| A | ILE35-GLY48 |
| site_id | PS00168 |
| Number of Residues | 15 |
| Details | TRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LvHgGAHKtNnaIgQ |
| Chain | Residue | Details |
| B | LEU75-GLN89 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| B | LYS82 | |
| I | ASP47 | |
| K | GLU36 | |
| K | ASP47 | |
| D | LYS82 | |
| F | LYS82 | |
| H | LYS82 | |
| J | LYS82 | |
| L | LYS82 | |
| G | GLU36 | |
| G | ASP47 | |
| I | GLU36 |
Catalytic Information from CSA
| site_id | CSA1 |
| 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 | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| H | LYS82 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| J | LYS82 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| L | LYS82 |
| site_id | CSA13 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| A | ALA141 |
| site_id | CSA14 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| C | ALA141 |
| site_id | CSA15 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| E | ALA141 |
| site_id | CSA16 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| G | ALA141 |
| site_id | CSA17 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| I | ALA141 |
| site_id | CSA18 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| K | ALA141 |
| site_id | CSA19 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| A | ASP47 | |
| A | TYR161 | |
| A | GLU36 |
| site_id | CSA2 |
| 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 | CSA20 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| C | ASP47 | |
| C | TYR161 | |
| C | GLU36 |
| site_id | CSA21 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| E | ASP47 | |
| E | TYR161 | |
| E | GLU36 |
| site_id | CSA22 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| G | ASP47 | |
| G | TYR161 | |
| G | GLU36 |
| site_id | CSA23 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| I | ASP47 | |
| I | TYR161 | |
| I | GLU36 |
| site_id | CSA24 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| K | ASP47 | |
| K | TYR161 | |
| K | GLU36 |
| site_id | CSA25 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| B | LYS82 | |
| B | SER371 |
| site_id | CSA26 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| D | LYS82 | |
| D | SER371 |
| site_id | CSA27 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| F | LYS82 | |
| F | SER371 |
| site_id | CSA28 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| H | LYS82 | |
| H | SER371 |
| site_id | CSA29 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| J | LYS82 | |
| J | SER371 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| F | HIS81 | |
| F | ASP300 | |
| F | LYS82 | |
| F | LYS162 |
| site_id | CSA30 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| L | LYS82 | |
| L | SER371 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| H | HIS81 | |
| H | ASP300 | |
| H | LYS82 | |
| H | LYS162 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| J | HIS81 | |
| J | ASP300 | |
| J | LYS82 | |
| J | LYS162 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| L | HIS81 | |
| L | ASP300 | |
| L | LYS82 | |
| L | LYS162 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| B | 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 | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| F | LYS82 |
