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 | 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 | 0016757 | molecular_function | glycosyltransferase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000105 | biological_process | L-histidine biosynthetic process |
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 | 0016757 | molecular_function | glycosyltransferase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0000105 | biological_process | L-histidine biosynthetic process |
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 | 0016757 | molecular_function | glycosyltransferase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000105 | biological_process | L-histidine biosynthetic process |
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 | 0016757 | molecular_function | glycosyltransferase activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0000105 | biological_process | L-histidine biosynthetic process |
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 | 0016757 | molecular_function | glycosyltransferase activity |
E | 0046872 | molecular_function | metal ion binding |
F | 0000105 | biological_process | L-histidine biosynthetic process |
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 | 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 |