6AMH
Engineered tryptophan synthase b-subunit from Pyrococcus furiosus, PfTrpB4D11 with Ser bound as E(Aex1)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000162 | biological_process | tryptophan biosynthetic process |
A | 0004834 | molecular_function | tryptophan synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006568 | biological_process | tryptophan metabolic process |
A | 0016829 | molecular_function | lyase activity |
B | 0000162 | biological_process | tryptophan biosynthetic process |
B | 0004834 | molecular_function | tryptophan synthase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006568 | biological_process | tryptophan metabolic process |
B | 0016829 | molecular_function | lyase activity |
C | 0000162 | biological_process | tryptophan biosynthetic process |
C | 0004834 | molecular_function | tryptophan synthase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006568 | biological_process | tryptophan metabolic process |
C | 0016829 | molecular_function | lyase activity |
D | 0000162 | biological_process | tryptophan biosynthetic process |
D | 0004834 | molecular_function | tryptophan synthase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006568 | biological_process | tryptophan metabolic process |
D | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | binding site for residue PLS A 401 |
Chain | Residue |
A | HIS81 |
A | GLY227 |
A | GLY228 |
A | GLY229 |
A | SER230 |
A | ASN231 |
A | GLY298 |
A | ASP300 |
A | GLU345 |
A | SER371 |
A | HOH512 |
A | LYS82 |
A | HOH559 |
A | THR105 |
A | GLY106 |
A | ALA107 |
A | GLY108 |
A | GLN109 |
A | HIS110 |
A | SER185 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue NA A 402 |
Chain | Residue |
A | GLY227 |
A | SER263 |
A | SER265 |
A | TYR301 |
A | GLY303 |
A | HOH506 |
A | HOH602 |
site_id | AC3 |
Number of Residues | 20 |
Details | binding site for residue PLS B 401 |
Chain | Residue |
B | HIS81 |
B | LYS82 |
B | THR105 |
B | GLY106 |
B | ALA107 |
B | GLY108 |
B | GLN109 |
B | HIS110 |
B | SER185 |
B | GLY227 |
B | GLY228 |
B | GLY229 |
B | SER230 |
B | ASN231 |
B | GLY298 |
B | ASP300 |
B | GLU345 |
B | SER371 |
B | HOH507 |
B | HOH576 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue NA B 402 |
Chain | Residue |
B | SER263 |
B | SER265 |
B | TYR301 |
B | GLY303 |
B | HOH577 |
site_id | AC5 |
Number of Residues | 20 |
Details | binding site for residue PLS C 401 |
Chain | Residue |
C | HIS81 |
C | LYS82 |
C | THR105 |
C | GLY106 |
C | ALA107 |
C | GLY108 |
C | GLN109 |
C | HIS110 |
C | SER185 |
C | GLY227 |
C | GLY228 |
C | GLY229 |
C | SER230 |
C | ASN231 |
C | GLY298 |
C | ASP300 |
C | GLU345 |
C | SER371 |
C | HOH510 |
C | HOH563 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue NA C 402 |
Chain | Residue |
C | SER263 |
C | SER265 |
C | TYR301 |
C | GLY303 |
C | HOH515 |
C | HOH558 |
site_id | AC7 |
Number of Residues | 21 |
Details | binding site for residue PLS D 401 |
Chain | Residue |
D | HIS81 |
D | LYS82 |
D | THR105 |
D | GLY106 |
D | ALA107 |
D | GLY108 |
D | GLN109 |
D | HIS110 |
D | SER185 |
D | GLY227 |
D | GLY228 |
D | GLY229 |
D | SER230 |
D | ASN231 |
D | PRO297 |
D | GLY298 |
D | ASP300 |
D | GLU345 |
D | SER371 |
D | HOH518 |
D | HOH551 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue NA D 402 |
Chain | Residue |
D | SER263 |
D | SER265 |
D | TYR301 |
D | GLY303 |
D | HOH560 |
D | HOH594 |
Functional Information from PROSITE/UniProt
site_id | PS00168 |
Number of Residues | 15 |
Details | TRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LvHgGAHKtNnaIgQ |
Chain | Residue | Details |
A | LEU75-GLN89 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS82 | |
B | LYS82 | |
C | LYS82 | |
D | LYS82 |