4YB6
Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni in complex with the inhibitors AMP and 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 | 13 |
Details | binding site for residue AMP A 301 |
Chain | Residue |
A | CYS104 |
A | HOH426 |
A | HOH446 |
A | HOH475 |
D | HIS33 |
A | ASP169 |
A | LEU170 |
A | VAL171 |
A | SER172 |
A | SER173 |
A | GLY174 |
A | ALA175 |
A | THR176 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue HIS A 302 |
Chain | Residue |
A | GLY247 |
A | VAL248 |
A | GLU249 |
A | ARG250 |
A | THR252 |
A | HIS266 |
A | VAL268 |
A | HOH418 |
E | HIS232 |
E | LEU256 |
E | SER288 |
E | LEU290 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue PEG A 303 |
Chain | Residue |
A | VAL185 |
A | VAL187 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG A 304 |
Chain | Residue |
A | ASP56 |
A | HOH508 |
A | HOH509 |
A | HOH510 |
A | HOH511 |
A | HOH512 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue AMP B 301 |
Chain | Residue |
B | CYS104 |
B | LEU170 |
B | SER172 |
B | SER173 |
B | GLY174 |
B | ALA175 |
B | THR176 |
B | HOH416 |
B | HOH435 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue HIS B 302 |
Chain | Residue |
B | GLY247 |
B | VAL248 |
B | GLU249 |
B | ARG250 |
B | THR252 |
B | HIS266 |
B | VAL268 |
B | HOH423 |
C | HIS232 |
C | LEU256 |
C | SER288 |
C | LEU290 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue PEG B 303 |
Chain | Residue |
B | ARG105 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue MG B 304 |
Chain | Residue |
B | ASP56 |
B | HOH446 |
B | HOH497 |
site_id | AC9 |
Number of Residues | 13 |
Details | binding site for residue AMP C 301 |
Chain | Residue |
C | CYS104 |
C | LEU170 |
C | SER172 |
C | SER173 |
C | GLY174 |
C | ALA175 |
C | THR176 |
C | HOH413 |
C | HOH426 |
C | HOH437 |
C | HOH445 |
C | HOH470 |
C | HOH519 |
site_id | AD1 |
Number of Residues | 11 |
Details | binding site for residue HIS C 302 |
Chain | Residue |
C | GLY247 |
C | VAL248 |
C | GLU249 |
C | ARG250 |
C | THR252 |
C | HIS266 |
C | VAL268 |
C | HOH419 |
F | HIS232 |
F | LEU256 |
F | SER288 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue PEG C 303 |
Chain | Residue |
C | ARG105 |
C | GLU184 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue MG C 304 |
Chain | Residue |
C | ASP56 |
C | HOH515 |
C | HOH516 |
C | HOH517 |
C | HOH518 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue MG C 305 |
Chain | Residue |
C | HOH476 |
C | HOH519 |
site_id | AD5 |
Number of Residues | 11 |
Details | binding site for residue AMP D 301 |
Chain | Residue |
D | THR176 |
D | HOH453 |
D | HOH489 |
D | GLY102 |
D | CYS104 |
D | ASP169 |
D | LEU170 |
D | SER172 |
D | SER173 |
D | GLY174 |
D | ALA175 |
site_id | AD6 |
Number of Residues | 11 |
Details | binding site for residue HIS D 302 |
Chain | Residue |
A | HIS232 |
A | SER288 |
A | LEU290 |
D | GLY247 |
D | VAL248 |
D | GLU249 |
D | ARG250 |
D | THR252 |
D | HIS266 |
D | VAL268 |
D | HOH423 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue PEG D 303 |
Chain | Residue |
D | ARG105 |
D | VAL185 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue MG D 304 |
Chain | Residue |
D | ASP56 |
D | HOH521 |
D | HOH522 |
D | HOH523 |
D | HOH524 |
D | HOH530 |
site_id | AD9 |
Number of Residues | 15 |
Details | binding site for residue AMP E 301 |
Chain | Residue |
E | GLY102 |
E | CYS104 |
E | ASP169 |
E | LEU170 |
E | VAL171 |
E | SER172 |
E | SER173 |
E | GLY174 |
E | ALA175 |
E | THR176 |
E | HOH417 |
E | HOH423 |
E | HOH501 |
E | HOH504 |
E | HOH505 |
site_id | AE1 |
Number of Residues | 12 |
Details | binding site for residue HIS E 302 |
Chain | Residue |
D | HIS232 |
D | LEU256 |
D | SER288 |
D | LEU290 |
E | GLY247 |
E | VAL248 |
E | GLU249 |
E | ARG250 |
E | THR252 |
E | HIS266 |
E | VAL268 |
E | HOH415 |
site_id | AE2 |
Number of Residues | 3 |
Details | binding site for residue PEG E 303 |
Chain | Residue |
E | ARG105 |
E | VAL185 |
E | VAL187 |
site_id | AE3 |
Number of Residues | 6 |
Details | binding site for residue MG E 304 |
Chain | Residue |
E | ASP56 |
E | HOH494 |
E | HOH495 |
E | HOH496 |
E | HOH497 |
E | HOH498 |
site_id | AE4 |
Number of Residues | 7 |
Details | binding site for residue MG E 305 |
Chain | Residue |
E | ALA223 |
E | GLU225 |
E | SER226 |
E | ILE294 |
E | HOH427 |
E | HOH481 |
E | HOH499 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue MG E 306 |
Chain | Residue |
E | HOH456 |
E | HOH502 |
E | HOH505 |
E | HOH506 |
site_id | AE6 |
Number of Residues | 14 |
Details | binding site for residue AMP F 301 |
Chain | Residue |
F | CYS104 |
F | LEU170 |
F | VAL171 |
F | SER172 |
F | SER173 |
F | GLY174 |
F | ALA175 |
F | THR176 |
F | HOH415 |
F | HOH474 |
F | HOH476 |
F | HOH481 |
F | HOH482 |
F | HOH491 |
site_id | AE7 |
Number of Residues | 12 |
Details | binding site for residue HIS F 302 |
Chain | Residue |
B | HIS232 |
B | LEU256 |
B | SER288 |
B | LEU290 |
F | GLY247 |
F | VAL248 |
F | GLU249 |
F | ARG250 |
F | THR252 |
F | HIS266 |
F | VAL268 |
F | HOH414 |
site_id | AE8 |
Number of Residues | 2 |
Details | binding site for residue PEG F 303 |
Chain | Residue |
F | ARG105 |
F | VAL187 |
site_id | AE9 |
Number of Residues | 4 |
Details | binding site for residue MG F 304 |
Chain | Residue |
F | ASP56 |
F | HOH508 |
F | HOH509 |
F | HOH510 |
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 |