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 |