5KIN
Crystal structure of tryptophan synthase alpha beta complex from Streptococcus pneumoniae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000162 | biological_process | tryptophan biosynthetic process |
A | 0004834 | molecular_function | tryptophan synthase activity |
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 | 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 | 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 | 0006568 | biological_process | tryptophan metabolic process |
D | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue GOL A 301 |
Chain | Residue |
A | ILE128 |
A | LEU131 |
A | ILE151 |
A | PRO152 |
A | LEU153 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue GOL C 301 |
Chain | Residue |
C | LEU153 |
C | ILE127 |
C | ILE128 |
C | LEU131 |
C | ILE151 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL D 501 |
Chain | Residue |
D | THR69 |
D | GLY74 |
D | LYS76 |
D | PRO372 |
Functional Information from PROSITE/UniProt
site_id | PS00167 |
Number of Residues | 14 |
Details | TRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. IEVGiPFSDPVADG |
Chain | Residue | Details |
A | ILE51-GLY64 |
site_id | PS00168 |
Number of Residues | 15 |
Details | TRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LnHtGAHKiNnaLgQ |
Chain | Residue | Details |
B | LEU84-GLN98 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00133 |
Chain | Residue | Details |
B | LLP91 | |
D | LLP91 | |
C | GLU52 | |
C | ASP63 |