6VFD
Tryptophan synthase mutant Q114A in complex with cesium ion at the metal coordination site and 2-aminophenol quinonoid at the enzyme beta site
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 | 7 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | PHE107 |
| A | ASN108 |
| A | HOH421 |
| A | HOH483 |
| A | HOH536 |
| B | ARG275 |
| B | VAL276 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | ILE64 |
| A | TYR175 |
| A | GLY234 |
| A | HOH546 |
| A | PHE22 |
| A | GLU49 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SER A 303 |
| Chain | Residue |
| A | PHE82 |
| A | PHE114 |
| A | ARG117 |
| A | HOH406 |
| A | HOH454 |
| A | HOH455 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 304 |
| Chain | Residue |
| A | ILE41 |
| A | HIS92 |
| A | PRO93 |
| A | THR94 |
| A | ILE95 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| A | ALA167 |
| A | GLY170 |
| A | HIS204 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 306 |
| Chain | Residue |
| A | HOH546 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | binding site for residue 1D0 B 401 |
| Chain | Residue |
| B | ALA85 |
| B | HIS86 |
| B | LYS87 |
| B | GLU109 |
| B | THR110 |
| B | GLY111 |
| B | GLY113 |
| B | ALA114 |
| B | HIS115 |
| B | THR190 |
| B | CYS230 |
| B | GLY232 |
| B | GLY233 |
| B | GLY234 |
| B | SER235 |
| B | ASN236 |
| B | GLY303 |
| B | GLU350 |
| B | SER377 |
| B | HOH601 |
| B | HOH604 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SER B 402 |
| Chain | Residue |
| B | TYR8 |
| B | PHE9 |
| B | GLY10 |
| B | TYR315 |
| B | HOH621 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | THR289 |
| B | ALA290 |
| B | ASP291 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | LYS219 |
| B | GLU220 |
| B | CL430 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue DMS B 405 |
| Chain | Residue |
| B | ILE262 |
| B | HIS267 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue DMS B 406 |
| Chain | Residue |
| B | GLU331 |
| B | HOH780 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 407 |
| Chain | Residue |
| B | SER143 |
| B | PRO144 |
| B | PHE147 |
| B | PHE385 |
| B | HIS388 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 408 |
| Chain | Residue |
| B | TYR8 |
| B | GLY10 |
| B | HOH774 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue DMS B 409 |
| Chain | Residue |
| B | LYS50 |
| B | GLY54 |
| B | ARG55 |
| B | PRO56 |
| B | THR57 |
| B | GLN215 |
| B | CS416 |
| B | CS416 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 410 |
| Chain | Residue |
| B | LEU271 |
| B | ARG363 |
| B | GLU364 |
| B | HOH815 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 411 |
| Chain | Residue |
| B | GLN42 |
| B | ALA46 |
| B | MET207 |
| B | HOH854 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 412 |
| Chain | Residue |
| B | THR3 |
| B | LEU4 |
| B | LEU5 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 413 |
| Chain | Residue |
| B | GLU211 |
| B | HOH681 |
| B | HOH846 |
| B | HOH894 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue CS B 414 |
| Chain | Residue |
| B | THR66 |
| B | THR69 |
| B | THR71 |
| site_id | AE3 |
| Number of Residues | 7 |
| Details | binding site for residue CS B 415 |
| Chain | Residue |
| B | GLY232 |
| B | GLU256 |
| B | GLY268 |
| B | LEU304 |
| B | PHE306 |
| B | SER308 |
| B | VAL231 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue CS B 416 |
| Chain | Residue |
| B | GLY54 |
| B | GLY54 |
| B | PRO56 |
| B | PRO56 |
| B | DMS409 |
| B | DMS409 |
| site_id | AE5 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 417 |
| Chain | Residue |
| B | GLN36 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 419 |
| Chain | Residue |
| B | ASP225 |
| B | SER249 |
| site_id | AE7 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 420 |
| Chain | Residue |
| B | HOH776 |
| site_id | AE8 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 421 |
| Chain | Residue |
| B | HOH533 |
| B | HOH720 |
| B | HOH958 |
| site_id | AE9 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 422 |
| Chain | Residue |
| B | ARG321 |
| B | HOH952 |
| site_id | AF1 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 424 |
| Chain | Residue |
| B | GLU155 |
| site_id | AF2 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 426 |
| Chain | Residue |
| B | GLN36 |
| B | LYS37 |
| site_id | AF3 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 427 |
| Chain | Residue |
| B | GLU369 |
| B | HOH515 |
| B | HOH672 |
| B | HOH779 |
| site_id | AF4 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 428 |
| Chain | Residue |
| B | THR248 |
| B | HOH904 |
| site_id | AF5 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 429 |
| Chain | Residue |
| B | HOH516 |
| site_id | AF6 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 430 |
| Chain | Residue |
| B | LYS219 |
| B | EDO404 |
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_FI3 |
| 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 |
