6BMA
The crystal structure of indole-3-glycerol phosphate synthase from Campylobacter jejuni subsp. jejuni NCTC 11168
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | tryptophan biosynthetic process |
| A | 0004425 | molecular_function | indole-3-glycerol-phosphate synthase activity |
| A | 0004640 | molecular_function | phosphoribosylanthranilate isomerase activity |
| A | 0006568 | biological_process | tryptophan metabolic process |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0000162 | biological_process | tryptophan biosynthetic process |
| B | 0004425 | molecular_function | indole-3-glycerol-phosphate synthase activity |
| B | 0004640 | molecular_function | phosphoribosylanthranilate isomerase activity |
| B | 0006568 | biological_process | tryptophan metabolic process |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue K A 301 |
| Chain | Residue |
| A | TYR110 |
| A | TYR110 |
| A | TYR110 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ARG109 |
| A | ARG109 |
| A | ARG109 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 303 |
| Chain | Residue |
| A | GLY241 |
| A | GLU242 |
| A | HOH417 |
| A | LYS58 |
| A | ARG190 |
| A | GLU218 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue PO4 A 304 |
| Chain | Residue |
| A | LYS18 |
| A | TYR23 |
| A | ARG158 |
| A | HIS159 |
| A | HOH409 |
| A | HOH424 |
| A | HOH449 |
| B | ASP123 |
| B | FMT310 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 A 305 |
| Chain | Residue |
| A | HIS229 |
| A | ASN232 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 306 |
| Chain | Residue |
| A | PRO22 |
| A | TYR23 |
| A | ASP24 |
| A | HOH401 |
| A | HOH403 |
| A | HOH430 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 307 |
| Chain | Residue |
| A | ASN79 |
| A | LYS82 |
| A | LYS98 |
| A | ASP249 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 308 |
| Chain | Residue |
| A | LYS84 |
| A | HOH448 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue K B 301 |
| Chain | Residue |
| B | TYR110 |
| B | TYR110 |
| B | TYR110 |
| B | CL302 |
| B | CL302 |
| B | CL302 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CL B 302 |
| Chain | Residue |
| B | ARG109 |
| B | ARG109 |
| B | ARG109 |
| B | K301 |
| B | K301 |
| B | K301 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 B 303 |
| Chain | Residue |
| A | ASP123 |
| B | LYS18 |
| B | TYR23 |
| B | ARG158 |
| B | HIS159 |
| B | HOH407 |
| B | HOH464 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 B 304 |
| Chain | Residue |
| B | LYS58 |
| B | GLY220 |
| B | ILE240 |
| B | GLY241 |
| B | GLU242 |
| B | HOH422 |
| B | HOH423 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 B 305 |
| Chain | Residue |
| B | ASN79 |
| B | LYS82 |
| B | ASN83 |
| B | LYS98 |
| B | ASP249 |
| B | GLY251 |
| B | HOH437 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 B 306 |
| Chain | Residue |
| B | PRO22 |
| B | TYR23 |
| B | ASP24 |
| B | HOH402 |
| B | HOH420 |
| B | HOH421 |
| B | HOH448 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 307 |
| Chain | Residue |
| B | PHE36 |
| B | LYS38 |
| B | ASP39 |
| B | LYS42 |
| B | HOH438 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue ACT B 308 |
| Chain | Residue |
| A | GLU193 |
| B | ALA0 |
| B | MET1 |
| B | LEU3 |
| B | ASP4 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 309 |
| Chain | Residue |
| B | LYS58 |
| B | PHE195 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue FMT B 310 |
| Chain | Residue |
| A | PO4304 |
| B | ASP123 |
| B | GLU124 |
| B | GLU149 |
| B | LYS152 |
Functional Information from PROSITE/UniProt
| site_id | PS00614 |
| Number of Residues | 19 |
| Details | IGPS Indole-3-glycerol phosphate synthase signature. IIaEVKKASPSkgviredF |
| Chain | Residue | Details |
| A | ILE53-PHE71 |
