6WDU
The external aldimine form of the Salmonella thypi wild-type tryptophan synthase in open conformation showing multiple side chain conformations for the residue beta Q114 and sodium ion at the metal coordination site. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | L-tryptophan biosynthetic process |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004834 | molecular_function | tryptophan synthase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006568 | biological_process | L-tryptophan metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| B | 0000162 | biological_process | L-tryptophan biosynthetic process |
| B | 0004834 | molecular_function | tryptophan synthase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006568 | biological_process | L-tryptophan metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | ARG225 |
| A | ARG267 |
| B | LYS99 |
| B | HOH731 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | PHE258 |
| B | GLU182 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | THR94 |
| A | ILE95 |
| A | ILE41 |
| A | HIS92 |
| A | PRO93 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 304 |
| Chain | Residue |
| A | PHE82 |
| A | HOH479 |
| A | HOH508 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 305 |
| Chain | Residue |
| A | ASP60 |
| A | ALA129 |
| A | ILE153 |
| A | HOH428 |
| A | HOH655 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 306 |
| Chain | Residue |
| A | GLU5 |
| A | ASN147 |
| A | ILE148 |
| A | ALA149 |
| A | HOH484 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue PEG B 401 |
| Chain | Residue |
| B | GLY10 |
| B | GLU11 |
| B | PHE12 |
| B | LYS283 |
| B | HOH558 |
| B | HOH694 |
| B | HOH789 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | PRO56 |
| B | GLU211 |
| B | HOH526 |
| B | HOH723 |
| B | HOH768 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | PHE9 |
| B | TYR315 |
| B | HOH529 |
| B | HOH582 |
| B | HOH717 |
| B | HOH803 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue PEG B 404 |
| Chain | Residue |
| B | ASN51 |
| B | LEU59 |
| B | THR60 |
| B | LYS61 |
| B | GLN63 |
| B | LEU125 |
| B | LYS219 |
| B | HOH508 |
| B | HOH609 |
| B | HOH857 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| B | GLN36 |
| B | GLN42 |
| B | DMS414 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | LYS219 |
| B | GLU220 |
| B | GLY221 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 407 |
| Chain | Residue |
| B | GLY232 |
| B | PHE306 |
| B | SER308 |
| B | HOH628 |
| B | HOH704 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 408 |
| Chain | Residue |
| B | THR66 |
| B | THR69 |
| B | THR71 |
| B | HOH756 |
| B | HOH832 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 409 |
| Chain | Residue |
| B | GLU210 |
| B | DMS413 |
| B | HOH573 |
| B | HOH576 |
| B | HOH578 |
| site_id | AD7 |
| Number of Residues | 22 |
| Details | binding site for residue KOU B 410 |
| Chain | Residue |
| B | HIS86 |
| B | LYS87 |
| B | THR110 |
| B | GLY111 |
| B | ALA112 |
| B | GLY113 |
| B | GLN114 |
| B | HIS115 |
| B | THR190 |
| B | GLY232 |
| B | GLY233 |
| B | GLY234 |
| B | SER235 |
| B | ASN236 |
| B | GLY303 |
| B | ASP305 |
| B | GLU350 |
| B | SER377 |
| B | HOH501 |
| B | HOH650 |
| B | HOH651 |
| B | HOH799 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 411 |
| Chain | Residue |
| B | GLN42 |
| B | ALA46 |
| B | HOH723 |
| B | HOH901 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue DMS B 412 |
| Chain | Residue |
| B | LEU271 |
| B | ASN317 |
| B | ARG363 |
| B | GLU364 |
| B | DMS420 |
| B | HOH516 |
| B | HOH564 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue DMS B 413 |
| Chain | Residue |
| B | EDO409 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 414 |
| Chain | Residue |
| B | GLN36 |
| B | LYS37 |
| B | PRO39 |
| B | EDO405 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 415 |
| Chain | Residue |
| B | THR3 |
| B | LEU4 |
| B | LEU5 |
| site_id | AE4 |
| Number of Residues | 2 |
| Details | binding site for residue DMS B 416 |
| Chain | Residue |
| B | HOH861 |
| B | HOH866 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 417 |
| Chain | Residue |
| B | TYR8 |
| B | GLY10 |
| B | GLU11 |
| B | HOH581 |
| B | HOH788 |
| site_id | AE6 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 418 |
| Chain | Residue |
| B | ILE262 |
| B | HIS267 |
| B | HOH843 |
| site_id | AE7 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 419 |
| Chain | Residue |
| B | SER143 |
| B | PHE385 |
| B | HIS388 |
| site_id | AE8 |
| Number of Residues | 7 |
| Details | binding site for residue DMS B 420 |
| Chain | Residue |
| B | LEU271 |
| B | LYS272 |
| B | GLY274 |
| B | ARG275 |
| B | VAL276 |
| B | PRO285 |
| B | DMS412 |
| site_id | AE9 |
| Number of Residues | 8 |
| Details | binding site for residue DMS B 421 |
| Chain | Residue |
| A | PHE107 |
| A | PRO138 |
| A | PHE139 |
| B | TYR16 |
| B | LYS283 |
| B | HOH581 |
| B | HOH788 |
| B | HOH955 |
Functional Information from PROSITE/UniProt
| site_id | PS00167 |
| Number of Residues | 14 |
| Details | TRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. LELGvPFSDPLADG |
| Chain | Residue | Details |
| A | LEU48-GLY61 |
| site_id | PS00168 |
| Number of Residues | 15 |
| Details | TRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LlHgGAHKtNqvLgQ |
| Chain | Residue | Details |
| B | LEU80-GLN94 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 383 |
| Chain | Residue | Details |
| B | LYS87 | electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | GLU109 | |
| B | SER377 | hydrogen bond donor |
