6WX3
High resolution Tryptophan Synthase crystal structure from Salmonella typhimurium in complex with F9 inhibitor in the alpha-site, Cesium ion at the metal coordination site and internal aldimine form.
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 | 21 |
| Details | binding site for residue F9F A 301 |
| Chain | Residue |
| A | PHE22 |
| A | THR183 |
| A | GLY184 |
| A | PHE212 |
| A | GLY213 |
| A | ILE232 |
| A | GLY234 |
| A | SER235 |
| A | HOH424 |
| A | HOH439 |
| A | HOH525 |
| A | GLU49 |
| A | HOH676 |
| B | PRO18 |
| A | ALA59 |
| A | ILE64 |
| A | LEU100 |
| A | LEU127 |
| A | ALA129 |
| A | ILE153 |
| A | TYR175 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ALA167 |
| A | GLY170 |
| A | HIS204 |
| A | HOH491 |
| A | HOH612 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue PLP B 1401 |
| Chain | Residue |
| B | HIS86 |
| B | LYS87 |
| B | GLN114 |
| B | THR190 |
| B | CYS230 |
| B | GLY232 |
| B | GLY233 |
| B | GLY234 |
| B | SER235 |
| B | ASN236 |
| B | GLY303 |
| B | GLU350 |
| B | SER377 |
| B | GLY378 |
| B | HOH1594 |
| B | HOH1600 |
| B | HOH1646 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue CS B 1402 |
| Chain | Residue |
| B | VAL231 |
| B | GLY232 |
| B | GLU256 |
| B | GLY268 |
| B | PRO270 |
| B | LEU304 |
| B | PHE306 |
| B | SER308 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue BCN B 1403 |
| Chain | Residue |
| B | GLY259 |
| B | HIS260 |
| B | GLU263 |
| B | THR328 |
| B | ASP329 |
| B | ASP330 |
| B | HOH1514 |
| B | HOH1534 |
| B | HOH1643 |
| B | HOH1975 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue BCN B 1404 |
| Chain | Residue |
| B | THR248 |
| B | VAL250 |
| B | GLY251 |
| B | LEU252 |
| B | GLY320 |
| B | ARG321 |
| B | ASP323 |
| B | HOH1561 |
| B | HOH1563 |
| B | HOH1665 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue BCN B 1405 |
| Chain | Residue |
| B | THR289 |
| B | ALA290 |
| B | ASP291 |
| B | GLN293 |
| B | HOH1568 |
| B | HOH1725 |
| B | HOH1769 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue BCN B 1406 |
| Chain | Residue |
| B | LEU271 |
| B | LYS272 |
| B | GLY274 |
| B | PRO285 |
| B | ARG363 |
| B | GLU364 |
| B | HOH1599 |
| B | HOH1701 |
| B | HOH1732 |
| B | HOH1756 |
| B | HOH1960 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 1407 |
| Chain | Residue |
| B | ASP225 |
| B | GLU369 |
| B | GLN370 |
| B | HOH1561 |
| B | HOH1628 |
| B | HOH1630 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue DMS B 1408 |
| Chain | Residue |
| B | GLY10 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 1409 |
| Chain | Residue |
| B | THR3 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue CS B 1410 |
| Chain | Residue |
| B | THR71 |
| B | HOH1849 |
| B | HOH1873 |
| B | THR66 |
| B | THR69 |
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 |
