Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0003879 | molecular_function | ATP phosphoribosyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0003879 | molecular_function | ATP phosphoribosyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS33 |
| A | HIS35 |
| B | GLU78 |
| B | GLU81 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | binding site for residue PRT A 302 |
| Chain | Residue |
| A | ASP56 |
| A | ASN75 |
| A | VAL76 |
| A | GLY102 |
| A | TYR103 |
| A | CYS104 |
| A | ASP169 |
| A | LEU170 |
| A | SER172 |
| A | SER173 |
| A | GLY174 |
| A | ALA175 |
| A | THR176 |
| A | ZN303 |
| A | HOH401 |
| A | HOH406 |
| A | HOH414 |
| A | HOH423 |
| A | HOH431 |
| A | HOH434 |
| A | HOH435 |
| A | HOH455 |
| A | HOH470 |
| A | HOH471 |
| A | GLN12 |
| A | GLY15 |
| A | ARG16 |
| A | ARG54 |
| A | ASP55 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 303 |
| Chain | Residue |
| A | ASP55 |
| A | ASP56 |
| A | PRT302 |
| A | HOH423 |
| A | HOH434 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS33 |
| B | HIS35 |
| B | TYR103 |
| B | CL305 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | HIS35 |
| B | ASP100 |
| B | GLU225 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | binding site for residue PRT B 303 |
| Chain | Residue |
| B | GLN12 |
| B | GLY15 |
| B | ARG16 |
| B | ARG54 |
| B | ASP55 |
| B | ASP56 |
| B | GLY73 |
| B | ASN75 |
| B | VAL76 |
| B | GLY102 |
| B | TYR103 |
| B | CYS104 |
| B | LEU170 |
| B | VAL171 |
| B | SER172 |
| B | SER173 |
| B | GLY174 |
| B | ALA175 |
| B | THR176 |
| B | ZN304 |
| B | HOH402 |
| B | HOH403 |
| B | HOH411 |
| B | HOH421 |
| B | HOH451 |
| B | HOH457 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 304 |
| Chain | Residue |
| B | ASP55 |
| B | ASP56 |
| B | PRT303 |
| B | HOH402 |
| B | HOH451 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 305 |
| Chain | Residue |
| B | TYR103 |
| B | ZN301 |
Functional Information from PROSITE/UniProt
| site_id | PS01316 |
| Number of Residues | 22 |
| Details | ATP_P_PHORIBOSYLTR ATP phosphoribosyltransferase signature. EvapraNlAdaIcDLvsSGaTL |
| Chain | Residue | Details |
| A | GLU156-LEU177 | |
