Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

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	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	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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)