4YB5
Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni in complex with the allosteric inhibitor histidine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003879 | molecular_function | ATP phosphoribosyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003879 | molecular_function | ATP phosphoribosyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000105 | biological_process | L-histidine biosynthetic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003879 | molecular_function | ATP phosphoribosyltransferase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000105 | biological_process | L-histidine biosynthetic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003879 | molecular_function | ATP phosphoribosyltransferase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000105 | biological_process | L-histidine biosynthetic process |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0003879 | molecular_function | ATP phosphoribosyltransferase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0008652 | biological_process | amino acid biosynthetic process |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016757 | molecular_function | glycosyltransferase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000105 | biological_process | L-histidine biosynthetic process |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0003879 | molecular_function | ATP phosphoribosyltransferase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0008652 | biological_process | amino acid biosynthetic process |
| F | 0016740 | molecular_function | transferase activity |
| F | 0016757 | molecular_function | glycosyltransferase activity |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue SCN A 301 |
| Chain | Residue |
| A | ASP100 |
| A | MET221 |
| A | ARG224 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SCN A 302 |
| Chain | Residue |
| A | ASN181 |
| F | PRO159 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue K A 303 |
| Chain | Residue |
| A | GLN178 |
| A | ASN181 |
| F | ARG160 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue HIS A 304 |
| Chain | Residue |
| A | VAL248 |
| A | GLU249 |
| A | ARG250 |
| A | THR252 |
| A | HIS266 |
| A | MET267 |
| A | VAL268 |
| A | HOH407 |
| E | HIS232 |
| E | SER288 |
| A | GLY247 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue K A 305 |
| Chain | Residue |
| A | ARG160 |
| F | GLN178 |
| F | ASN181 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SCN B 301 |
| Chain | Residue |
| B | ASP100 |
| B | MET221 |
| B | ARG224 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue K B 302 |
| Chain | Residue |
| B | GLN178 |
| B | ASN181 |
| D | ARG160 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue HIS B 303 |
| Chain | Residue |
| B | GLY247 |
| B | VAL248 |
| B | GLU249 |
| B | ARG250 |
| B | THR252 |
| B | HIS266 |
| B | MET267 |
| B | VAL268 |
| C | HIS232 |
| C | SER288 |
| C | HOH403 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue SCN C 301 |
| Chain | Residue |
| C | MET221 |
| C | ARG224 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue PGE C 302 |
| Chain | Residue |
| C | SER226 |
| C | LEU245 |
| C | PRO246 |
| C | GLY247 |
| C | VAL248 |
| C | VAL268 |
| C | SER269 |
| C | LYS270 |
| C | LEU273 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue K C 303 |
| Chain | Residue |
| C | GLN178 |
| C | ASN181 |
| E | ARG160 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue HIS C 304 |
| Chain | Residue |
| C | GLY247 |
| C | VAL248 |
| C | GLU249 |
| C | ARG250 |
| C | THR252 |
| C | HIS266 |
| C | VAL268 |
| F | HIS232 |
| F | SER288 |
| F | HOH404 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue K C 305 |
| Chain | Residue |
| C | ARG160 |
| E | GLN178 |
| E | ASN181 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue PEG D 301 |
| Chain | Residue |
| D | LYS235 |
| D | PRO255 |
| D | LEU256 |
| D | ASP259 |
| D | ASN262 |
| D | VAL263 |
| site_id | AD6 |
| Number of Residues | 10 |
| Details | binding site for residue HIS D 302 |
| Chain | Residue |
| A | HIS232 |
| A | SER288 |
| D | GLY247 |
| D | VAL248 |
| D | GLU249 |
| D | ARG250 |
| D | THR252 |
| D | HIS266 |
| D | VAL268 |
| D | HOH404 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue SCN E 301 |
| Chain | Residue |
| E | ASP100 |
| E | PHE101 |
| E | MET221 |
| E | ARG224 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue SCN E 302 |
| Chain | Residue |
| C | PRO111 |
| C | PRO159 |
| C | HOH413 |
| E | ASN181 |
| site_id | AD9 |
| Number of Residues | 10 |
| Details | binding site for residue HIS E 303 |
| Chain | Residue |
| E | HOH405 |
| D | HIS232 |
| D | SER288 |
| E | GLY247 |
| E | VAL248 |
| E | GLU249 |
| E | ARG250 |
| E | THR252 |
| E | HIS266 |
| E | VAL268 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue SCN F 301 |
| Chain | Residue |
| F | ASP100 |
| F | MET221 |
| F | ARG224 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue SCN F 302 |
| Chain | Residue |
| D | HIS258 |
| F | LYS186 |
| F | VAL187 |
| site_id | AE3 |
| Number of Residues | 9 |
| Details | binding site for residue PEG F 303 |
| Chain | Residue |
| F | VAL220 |
| F | ALA223 |
| F | ARG224 |
| F | GLU225 |
| F | SER226 |
| F | LYS227 |
| F | PRO293 |
| F | ILE294 |
| F | GLU295 |
| site_id | AE4 |
| Number of Residues | 12 |
| Details | binding site for residue HIS F 304 |
| Chain | Residue |
| B | HIS232 |
| B | SER288 |
| B | LEU290 |
| F | GLY247 |
| F | VAL248 |
| F | GLU249 |
| F | ARG250 |
| F | THR252 |
| F | HIS266 |
| F | MET267 |
| F | VAL268 |
| F | HOH403 |
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 |
