1A5B
CRYO-CRYSTALLOGRAPHY OF A TRUE SUBSTRATE, INDOLE-3-GLYCEROL PHOSPHATE, BOUND TO A MUTANT (ALPHA D60N) TRYPTOPHAN SYNTHASE ALPHA2BETA2 COMPLEX REVEALS THE CORRECT ORIENTATION OF ACTIVE SITE ALPHA GLU 49
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000162 | biological_process | 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 | tryptophan metabolic process |
A | 0008152 | biological_process | 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 | 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 | 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 K B 500 |
Chain | Residue |
B | GLY232 |
B | GLY268 |
B | PHE306 |
B | SER308 |
B | HOH596 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE IGP A 271 |
Chain | Residue |
A | ASN60 |
A | LEU100 |
A | ILE153 |
A | TYR175 |
A | GLY211 |
A | GLY213 |
A | GLY234 |
A | SER235 |
A | HOH585 |
A | HOH586 |
A | GLU49 |
A | ALA59 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PLP B 501 |
Chain | Residue |
B | HIS86 |
B | LYS87 |
B | GLN114 |
B | THR190 |
B | GLY232 |
B | GLY233 |
B | GLY234 |
B | SER235 |
B | ASN236 |
B | GLY303 |
B | GLU350 |
B | SER377 |
B | GLY378 |
B | HOH598 |
B | HOH634 |
site_id | S1 |
Number of Residues | 1 |
Details | TRUE SUBSTRATE IGP IS BOUND TO THE ACTIVE SITE OF A-SUBUNIT. |
Chain | Residue |
A | IGP271 |
site_id | S2 |
Number of Residues | 1 |
Details | COENZYME PLP BINDING SITE. |
Chain | Residue |
B | PLP501 |
Functional Information from PROSITE/UniProt
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 | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
B | THR88 | |
A | ASN60 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 383 |
Chain | Residue | Details |
B | THR88 | electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
B | THR110 | |
B | GLY378 | hydrogen bond donor |