2TRS
CRYSTAL STRUCTURES OF MUTANT (BETAK87T) TRYPTOPHAN SYNTHASE ALPHA2 BETA2 COMPLEX WITH LIGANDS BOUND TO THE ACTIVE SITES OF THE ALPHA AND BETA SUBUNITS REVEAL LIGAND-INDUCED CONFORMATIONAL CHANGES
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 | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 400 |
| Chain | Residue |
| B | GLY232 |
| B | PHE306 |
| B | SER308 |
| B | HOH418 |
| B | HOH483 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IPL A 273 |
| Chain | Residue |
| A | TYR175 |
| A | THR183 |
| A | GLY184 |
| A | PHE212 |
| A | GLY213 |
| A | GLY234 |
| A | SER235 |
| A | ALA59 |
| A | ASP60 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PLS B 398 |
| Chain | Residue |
| B | HIS86 |
| B | THR110 |
| B | GLY111 |
| B | ALA112 |
| B | GLY113 |
| B | GLN114 |
| B | HIS115 |
| B | THR190 |
| B | GLY232 |
| B | GLY233 |
| B | GLY234 |
| B | SER235 |
| B | ASN236 |
| B | ALA302 |
| B | GLY303 |
| B | LEU304 |
| B | SER377 |
| B | LYS382 |
| B | HOH441 |
| B | HOH541 |
| site_id | S1 |
| Number of Residues | 1 |
| Details | SUBSTRATE ANALOG BOUND TO THE ALPHA ACTIVE SITE. |
| Chain | Residue |
| A | IPL273 |
| site_id | S2 |
| Number of Residues | 1 |
| Details | REACTION INTERMEDIATE BOUND TO THE BETA ACTIVE SITE. |
| Chain | Residue |
| B | PLS398 |
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 |
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 | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| B | HIS86 | |
| B | THR87 | |
| B | LYS167 | |
| B | ASP305 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| B | THR87 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a50 |
| Chain | Residue | Details |
| A | TYR175 | |
| A | GLU49 | |
| A | ASP60 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 383 |
| Chain | Residue | Details |
| B | THR87 | electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | GLU109 | |
| B | SER377 | hydrogen bond donor |
