4HPX
Crystal structure of Tryptophan Synthase at 1.65 A resolution in complex with alpha aminoacrylate E(A-A) and benzimidazole in the beta site and the F9 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 | 20 |
| 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 | HOH431 |
| A | HOH522 |
| A | HOH523 |
| A | GLU49 |
| B | PRO18 |
| A | ALA59 |
| A | ILE64 |
| A | LEU100 |
| A | LEU127 |
| A | ALA129 |
| A | ILE153 |
| A | TYR175 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG A 302 |
| Chain | Residue |
| A | ARG164 |
| A | SER168 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BZI B 401 |
| Chain | Residue |
| B | LYS87 |
| B | GLU109 |
| B | LEU166 |
| B | GLY189 |
| B | THR190 |
| B | GLY233 |
| B | PHE306 |
| B | 0JO404 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BZI B 402 |
| Chain | Residue |
| B | THR3 |
| B | LEU4 |
| B | LEU5 |
| B | ASN6 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BZI B 403 |
| Chain | Residue |
| B | LYS137 |
| B | HOH845 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 0JO B 404 |
| Chain | Residue |
| B | HIS86 |
| B | LYS87 |
| 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 | BZI401 |
| B | HOH505 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BCN B 405 |
| Chain | Residue |
| B | THR248 |
| B | SER249 |
| B | VAL250 |
| B | GLY251 |
| B | LEU252 |
| B | GLY320 |
| B | ARG321 |
| B | ASP323 |
| B | HOH607 |
| B | HOH629 |
| B | HOH758 |
| B | HOH805 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BCN B 406 |
| Chain | Residue |
| B | GLY259 |
| B | HIS260 |
| B | GLU263 |
| B | THR328 |
| B | ASP329 |
| B | ASP330 |
| B | PEG408 |
| B | HOH533 |
| B | HOH635 |
| B | HOH734 |
| B | HOH769 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCN B 407 |
| Chain | Residue |
| B | THR289 |
| B | ALA290 |
| B | ASP291 |
| B | GLN293 |
| B | HOH573 |
| B | HOH632 |
| B | HOH930 |
| B | HOH932 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG B 408 |
| Chain | Residue |
| B | GLU263 |
| B | THR264 |
| B | BCN406 |
| B | HOH714 |
| B | HOH772 |
| B | HOH910 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 409 |
| Chain | Residue |
| B | HOH740 |
| B | ILE262 |
| B | GLU263 |
| B | THR264 |
| B | GLY265 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 410 |
| Chain | Residue |
| B | GLU211 |
| B | ALA214 |
| B | HOH660 |
| B | HOH870 |
| B | HOH921 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG B 411 |
| Chain | Residue |
| B | GLY179 |
| B | SER180 |
| B | TYR181 |
| B | GLU182 |
| B | THR183 |
| B | HOH832 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CS B 412 |
| Chain | Residue |
| B | GLY232 |
| B | GLY268 |
| B | LEU304 |
| B | PHE306 |
| B | SER308 |
| B | HOH946 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CS B 413 |
| Chain | Residue |
| B | THR66 |
| B | THR69 |
| B | THR71 |
| B | HOH938 |
| B | HOH948 |
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 |
