Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4TWB

Sulfolobus solfataricus ribose-phosphate pyrophosphokinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0002189	cellular_component	ribose phosphate diphosphokinase complex
A	0004749	molecular_function	ribose phosphate diphosphokinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0009165	biological_process	nucleotide biosynthetic process
A	0016301	molecular_function	kinase activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0002189	cellular_component	ribose phosphate diphosphokinase complex
B	0004749	molecular_function	ribose phosphate diphosphokinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0009165	biological_process	nucleotide biosynthetic process
B	0016301	molecular_function	kinase activity
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0002189	cellular_component	ribose phosphate diphosphokinase complex
C	0004749	molecular_function	ribose phosphate diphosphokinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
C	0006164	biological_process	purine nucleotide biosynthetic process
C	0009165	biological_process	nucleotide biosynthetic process
C	0016301	molecular_function	kinase activity
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0002189	cellular_component	ribose phosphate diphosphokinase complex
D	0004749	molecular_function	ribose phosphate diphosphokinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
D	0006164	biological_process	purine nucleotide biosynthetic process
D	0009165	biological_process	nucleotide biosynthetic process
D	0016301	molecular_function	kinase activity
D	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0002189	cellular_component	ribose phosphate diphosphokinase complex
E	0004749	molecular_function	ribose phosphate diphosphokinase activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
E	0006164	biological_process	purine nucleotide biosynthetic process
E	0009165	biological_process	nucleotide biosynthetic process
E	0016301	molecular_function	kinase activity
E	0046872	molecular_function	metal ion binding
F	0000287	molecular_function	magnesium ion binding
F	0002189	cellular_component	ribose phosphate diphosphokinase complex
F	0004749	molecular_function	ribose phosphate diphosphokinase activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006015	biological_process	5-phosphoribose 1-diphosphate biosynthetic process
F	0006164	biological_process	purine nucleotide biosynthetic process
F	0009165	biological_process	nucleotide biosynthetic process
F	0016301	molecular_function	kinase activity
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue AMP A 301

Chain	Residue
A	ARG93
A	GLN94
A	PHE98
A	HIS127
B	PHE32
B	ASP34
B	GLU36

site_id	AC2
Number of Residues	6
Details	binding site for residue SO4 A 302

Chain	Residue
A	THR221
A	GLY222
A	GLY223
A	THR224
A	ARG93
A	SER220

site_id	AC3
Number of Residues	7
Details	binding site for residue AMP A 303

Chain	Residue
A	PHE32
A	ASP34
A	GLU36
B	ARG93
B	GLN94
B	PHE98
B	HIS127

site_id	AC4
Number of Residues	6
Details	binding site for residue SO4 B 301

Chain	Residue
B	ARG93
B	SER220
B	THR221
B	GLY222
B	GLY223
B	THR224

site_id	AC5
Number of Residues	7
Details	binding site for residue AMP C 301

Chain	Residue
C	ARG93
C	GLN94
C	PHE98
C	HIS127
D	PHE32
D	ASP34
D	GLU36

site_id	AC6
Number of Residues	6
Details	binding site for residue SO4 C 302

Chain	Residue
C	ARG93
C	SER220
C	THR221
C	GLY222
C	GLY223
C	THR224

site_id	AC7
Number of Residues	7
Details	binding site for residue AMP C 303

Chain	Residue
C	PHE32
C	ASP34
C	GLU36
D	ARG93
D	GLN94
D	PHE98
D	HIS127

site_id	AC8
Number of Residues	7
Details	binding site for residue SO4 D 301

Chain	Residue
D	ARG93
D	ILE219
D	SER220
D	THR221
D	GLY222
D	GLY223
D	THR224

site_id	AC9
Number of Residues	6
Details	binding site for residue SO4 E 301

Chain	Residue
E	ARG93
E	SER220
E	THR221
E	GLY222
E	GLY223
E	THR224

site_id	AD1
Number of Residues	7
Details	binding site for residue AMP E 302

Chain	Residue
E	PHE32
E	ASP34
E	GLU36
F	ARG93
F	GLN94
F	PHE98
F	HIS127

site_id	AD2
Number of Residues	7
Details	binding site for residue AMP F 301

Chain	Residue
E	ARG93
E	GLN94
E	PHE98
E	HIS127
F	PHE32
F	ASP34
F	GLU36

site_id	AD3
Number of Residues	6
Details	binding site for residue SO4 F 302

Chain	Residue
F	ARG93
F	SER220
F	THR221
F	GLY222
F	GLY223
F	THR224

Functional Information from PROSITE/UniProt

site_id	PS00103
Number of Residues	13
Details	PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VVIIDDIISTGgT

Chain	Residue	Details
A	VAL212-THR224

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00583

Chain	Residue	Details
A	LYS188
B	LYS188
C	LYS188
D	LYS188
E	LYS188
F	LYS188

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00583, ECO:0000305\|PubMed:25605536, ECO:0007744\|PDB:4TWB

Chain	Residue	Details
A	ASP34
E	ARG93
F	ASP34
F	ARG93
A	ARG93
B	ASP34
B	ARG93
C	ASP34
C	ARG93
D	ASP34
D	ARG93
E	ASP34

site_id	SWS_FT_FI3
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00583

Chain	Residue	Details
A	HIS127
C	ASP165
C	ARG190
C	ASP216
D	HIS127
D	ASP165
D	ARG190
D	ASP216
E	HIS127
E	ASP165
E	ARG190
A	ASP165
E	ASP216
F	HIS127
F	ASP165
F	ARG190
F	ASP216
A	ARG190
A	ASP216
B	HIS127
B	ASP165
B	ARG190
B	ASP216
C	HIS127

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00583, ECO:0000269\|PubMed:25605536, ECO:0007744\|PDB:4TWB

Chain	Residue	Details
A	SER220
B	SER220
C	SER220
D	SER220
E	SER220
F	SER220

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