7LEV
The aminoacrylate form of the wild-type Salmonella typhimurium Tryptophan Synthase in complex with ammonium ion at the metal coordination site at 1.70 Angstrom resolution
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 DMS A 301 | 
| Chain | Residue | 
| A | ALA59 | 
| A | LEU100 | 
| A | ILE153 | 
| A | TYR175 | 
| site_id | AC2 | 
| Number of Residues | 7 | 
| Details | binding site for residue EDO A 302 | 
| Chain | Residue | 
| A | ASN147 | 
| A | HOH445 | 
| A | MET1 | 
| A | ARG3 | 
| A | GLU119 | 
| A | GLY122 | 
| A | VAL123 | 
| site_id | AC3 | 
| Number of Residues | 4 | 
| Details | binding site for residue EDO A 303 | 
| Chain | Residue | 
| A | PHE82 | 
| A | ALA113 | 
| A | HOH412 | 
| A | HOH454 | 
| site_id | AC4 | 
| Number of Residues | 4 | 
| Details | binding site for residue CL A 304 | 
| Chain | Residue | 
| A | HIS92 | 
| A | PRO93 | 
| A | THR94 | 
| A | ILE95 | 
| site_id | AC5 | 
| Number of Residues | 5 | 
| Details | binding site for residue DMS B 401 | 
| Chain | Residue | 
| B | LYS50 | 
| B | GLY54 | 
| B | ARG55 | 
| B | THR57 | 
| B | GLN215 | 
| site_id | AC6 | 
| Number of Residues | 3 | 
| Details | binding site for residue DMS B 402 | 
| Chain | Residue | 
| B | LEU271 | 
| B | ASN317 | 
| B | ARG363 | 
| site_id | AC7 | 
| Number of Residues | 2 | 
| Details | binding site for residue DMS B 403 | 
| Chain | Residue | 
| B | GLN42 | 
| B | MET207 | 
| site_id | AC8 | 
| Number of Residues | 3 | 
| Details | binding site for residue DMS B 404 | 
| Chain | Residue | 
| B | GLU211 | 
| B | GLN215 | 
| B | HOH549 | 
| site_id | AC9 | 
| Number of Residues | 1 | 
| Details | binding site for residue DMS B 405 | 
| Chain | Residue | 
| B | HOH527 | 
| site_id | AD1 | 
| Number of Residues | 21 | 
| Details | binding site for residue 0JO B 406 | 
| Chain | Residue | 
| B | ALA85 | 
| B | HIS86 | 
| B | LYS87 | 
| B | THR110 | 
| B | GLY111 | 
| B | ALA112 | 
| B | GLY113 | 
| B | GLN114 | 
| B | HIS115 | 
| B | THR190 | 
| B | CYS230 | 
| B | GLY232 | 
| B | GLY233 | 
| B | GLY234 | 
| B | SER235 | 
| B | ASN236 | 
| B | GLY303 | 
| B | GLU350 | 
| B | SER377 | 
| B | HOH574 | 
| B | HOH675 | 
| site_id | AD2 | 
| Number of Residues | 4 | 
| Details | binding site for residue DMS B 407 | 
| Chain | Residue | 
| B | ASP47 | 
| B | ASN51 | 
| B | THR60 | 
| B | LYS61 | 
| site_id | AD3 | 
| Number of Residues | 4 | 
| Details | binding site for residue DMS B 408 | 
| Chain | Residue | 
| B | THR66 | 
| B | THR69 | 
| B | THR71 | 
| B | HOH745 | 
| site_id | AD4 | 
| Number of Residues | 5 | 
| Details | binding site for residue EDO B 409 | 
| Chain | Residue | 
| B | PHE9 | 
| B | TYR315 | 
| B | HOH503 | 
| B | HOH581 | 
| B | HOH692 | 
| site_id | AD5 | 
| Number of Residues | 6 | 
| Details | binding site for residue NH4 B 410 | 
| Chain | Residue | 
| B | GLY232 | 
| B | GLY268 | 
| B | LEU304 | 
| B | PHE306 | 
| B | SER308 | 
| B | HOH526 | 
| site_id | AD6 | 
| Number of Residues | 2 | 
| Details | binding site for residue CL B 411 | 
| Chain | Residue | 
| B | GLN36 | 
| B | LYS37 | 
| site_id | AD7 | 
| Number of Residues | 2 | 
| Details | binding site for residue CL B 413 | 
| Chain | Residue | 
| B | LEU5 | 
| B | ASN6 | 
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 | 











