4KKX
Crystal structure of Tryptophan Synthase from Salmonella typhimurium with 2-aminophenol quinonoid in the beta site and the F6 inhibitor in the alpha 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 | 19 |
| Details | BINDING SITE FOR RESIDUE F6F A 301 |
| Chain | Residue |
| A | GLU49 |
| A | PHE212 |
| A | GLY213 |
| A | GLY234 |
| A | SER235 |
| A | HOH422 |
| A | HOH438 |
| A | HOH444 |
| B | PRO18 |
| B | HOH527 |
| B | HOH563 |
| A | ALA59 |
| A | ILE64 |
| A | LEU100 |
| A | ALA129 |
| A | ILE153 |
| A | TYR175 |
| A | THR183 |
| A | GLY184 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 302 |
| Chain | Residue |
| A | ASN104 |
| A | ASN108 |
| A | HOH691 |
| B | ARG275 |
| B | VAL276 |
| B | GLN288 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 303 |
| Chain | Residue |
| A | SER168 |
| A | HOH756 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PEG A 304 |
| Chain | Residue |
| A | ARG179 |
| A | GLY181 |
| A | VAL182 |
| A | THR183 |
| A | GLY184 |
| A | ASN187 |
| A | HOH437 |
| A | HOH508 |
| A | HOH512 |
| A | HOH761 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 305 |
| Chain | Residue |
| A | ARG15 |
| A | GLU16 |
| A | VAL224 |
| A | HOH773 |
| B | GLU40 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE AQ3 B 401 |
| Chain | Residue |
| B | HIS86 |
| B | LYS87 |
| B | GLU109 |
| B | THR110 |
| B | GLY111 |
| B | ALA112 |
| B | GLY113 |
| B | GLN114 |
| B | HIS115 |
| B | LEU166 |
| B | THR190 |
| B | CYS230 |
| B | GLY232 |
| B | GLY233 |
| B | GLY234 |
| B | SER235 |
| B | ASN236 |
| B | GLY303 |
| B | GLU350 |
| B | SER377 |
| B | GLY378 |
| B | NA403 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 402 |
| Chain | Residue |
| B | GLY232 |
| B | PHE306 |
| B | SER308 |
| B | HOH505 |
| B | HOH857 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA B 403 |
| Chain | Residue |
| B | CYS230 |
| B | VAL231 |
| B | GLY234 |
| B | SER235 |
| B | ASN236 |
| B | ALA237 |
| B | AQ3401 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 404 |
| Chain | Residue |
| B | LYS50 |
| B | GLN215 |
| B | LYS219 |
| B | PGE413 |
| B | HOH881 |
| B | HOH925 |
| B | HOH1029 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 405 |
| Chain | Residue |
| B | ASN6 |
| B | GLY10 |
| B | HOH623 |
| B | HOH627 |
| B | HOH791 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 406 |
| Chain | Residue |
| B | THR66 |
| B | THR69 |
| B | ARG70 |
| B | THR71 |
| B | HOH889 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 407 |
| Chain | Residue |
| B | HIS273 |
| B | VAL325 |
| B | SER326 |
| B | HOH608 |
| B | HOH765 |
| B | HOH811 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 408 |
| Chain | Residue |
| A | GLU134 |
| A | LEU162 |
| A | HOH468 |
| A | HOH635 |
| A | HOH687 |
| B | GLN19 |
| B | MET22 |
| B | PRO23 |
| B | ASN26 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 409 |
| Chain | Residue |
| B | LYS272 |
| B | GLU364 |
| B | HOH725 |
| B | HOH861 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 410 |
| Chain | Residue |
| B | ARG275 |
| B | VAL276 |
| B | HOH502 |
| B | HOH708 |
| B | HOH749 |
| B | HOH963 |
| B | HOH982 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 411 |
| Chain | Residue |
| B | THR3 |
| B | LEU5 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 412 |
| Chain | Residue |
| B | GLU266 |
| B | SER297 |
| B | TYR298 |
| B | HOH599 |
| B | HOH764 |
| B | HOH1021 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PGE B 413 |
| Chain | Residue |
| B | GLU210 |
| B | GLU211 |
| B | ALA214 |
| B | EDO404 |
| B | HOH738 |
| B | HOH745 |
| B | HOH819 |
| B | HOH936 |
| B | HOH957 |
| site_id | CC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PGE B 414 |
| Chain | Residue |
| B | ASP47 |
| B | ASN51 |
| B | TYR52 |
| B | LEU59 |
| B | THR60 |
| B | LYS61 |
| B | GLN63 |
| B | LEU125 |
| B | LYS219 |
| B | GLU343 |
| B | HOH557 |
| B | HOH673 |
| B | HOH776 |
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 |
