Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1USY

ATP phosphoribosyl transferase (HisG:HisZ) complex from Thermotoga maritima

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000105	biological_process	L-histidine biosynthetic process
A	0004821	molecular_function	histidine-tRNA ligase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006427	biological_process	histidyl-tRNA aminoacylation
A	0008652	biological_process	amino acid biosynthetic process
B	0000105	biological_process	L-histidine biosynthetic process
B	0004821	molecular_function	histidine-tRNA ligase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006427	biological_process	histidyl-tRNA aminoacylation
B	0008652	biological_process	amino acid biosynthetic process
C	0000105	biological_process	L-histidine biosynthetic process
C	0004821	molecular_function	histidine-tRNA ligase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006427	biological_process	histidyl-tRNA aminoacylation
C	0008652	biological_process	amino acid biosynthetic process
D	0000105	biological_process	L-histidine biosynthetic process
D	0004821	molecular_function	histidine-tRNA ligase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006427	biological_process	histidyl-tRNA aminoacylation
D	0008652	biological_process	amino acid biosynthetic process
E	0000105	biological_process	L-histidine biosynthetic process
E	0000166	molecular_function	nucleotide 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
F	0000105	biological_process	L-histidine biosynthetic process
F	0000166	molecular_function	nucleotide 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
G	0000105	biological_process	L-histidine biosynthetic process
G	0000166	molecular_function	nucleotide binding
G	0003879	molecular_function	ATP phosphoribosyltransferase activity
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0008652	biological_process	amino acid biosynthetic process
G	0016740	molecular_function	transferase activity
G	0016757	molecular_function	glycosyltransferase activity
H	0000105	biological_process	L-histidine biosynthetic process
H	0000166	molecular_function	nucleotide binding
H	0003879	molecular_function	ATP phosphoribosyltransferase activity
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0008652	biological_process	amino acid biosynthetic process
H	0016740	molecular_function	transferase activity
H	0016757	molecular_function	glycosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 E 1202

Chain	Residue
E	THR149
E	GLU150
E	THR151
E	GLY152
E	ARG153
E	THR154

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 E 1203

Chain	Residue
F	LYS8
E	LYS108
E	GLY131
E	SER132

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 F 1203

Chain	Residue
F	GLU150
F	THR151
F	GLY152
F	ARG153
F	THR154

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 G 1204

Chain	Residue
G	GLU150
G	THR151
G	GLY152
G	ARG153
G	THR154

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 G 1205

Chain	Residue
G	LYS108
G	GLY131
G	SER132
G	HOH2024
H	ARG45

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 H 1202

Chain	Residue
H	THR149
H	GLU150
H	THR151
H	GLY152
H	ARG153
H	THR154

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE HIS C 1275

Chain	Residue
C	LYS157
C	LEU159
C	ILE184
C	TYR185
G	PRO78
G	TYR180
G	GLN195

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HIS D 1276

Chain	Residue
D	TYR185
F	LEU191
F	GLN195

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE HIS E 1204

Chain	Residue
B	LYS157
B	ILE184
E	PRO78
E	TYR180
E	HOH2020

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HIS E 1205

Chain	Residue
B	GLU161
E	THR65
E	ARG170
E	HIS172

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE HIS F 1204

Chain	Residue
D	GLU161
F	THR65
F	LEU68
F	GLN77
F	ARG170
F	HIS172

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE HIS G 1206

Chain	Residue
C	ASN158
G	THR65
G	GLN77
G	ARG170
G	HIS172
G	HOH2025
G	HOH2026
G	HOH2027

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE HIS H 1203

Chain	Residue
A	ILE184
A	TYR185
H	ILE76
H	PRO78
H	TYR180
H	LEU191
H	GLN195

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE HIS H 1204

Chain	Residue
A	GLU161
A	HOH2023
H	THR65
H	GLN77
H	ARG170
H	HIS172

Functional Information from PROSITE/UniProt

site_id	PS01316
Number of Residues	22
Details	ATP_P_PHORIBOSYLTR ATP phosphoribosyltransferase signature. ElapiaGlSdlIvDIteTGrTL

Chain	Residue	Details
E	GLU134-LEU155
H	GLU134-LEU155

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