3MBI

Crystal structure of the phosphoribosylpyrophosphate (PRPP) synthetase from Thermoplasma volcanium in complex with ADP-Mg2+ and ribose 5-phosphate

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	0016310	biological_process	phosphorylation
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	0016310	biological_process	phosphorylation
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	0016310	biological_process	phosphorylation
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	0016310	biological_process	phosphorylation
D	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU206-THR218

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site_id	PS00144
Number of Residues	9
Details	ASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IiSTGGTIA

Chain	Residue	Details
A	ILE212-ALA220

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:21963988, ECO:0007744|PDB:3MBI

Chain	Residue	Details
A	LYS184
B	LYS184
C	LYS184
D	LYS184

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:21963988, ECO:0007744|PDB:3LPN, ECO:0007744|PDB:3LRT, ECO:0007744|PDB:3MBI, ECO:0007744|PDB:3NAG

Chain	Residue	Details
A	ASP34
A	SER214
B	ASP34
B	SER214
C	ASP34
C	SER214
D	ASP34
D	SER214

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:21963988, ECO:0007744|PDB:3LPN, ECO:0007744|PDB:3LRT, ECO:0007744|PDB:3MBI, ECO:0007744|PDB:3NAG

Chain	Residue	Details
A	ARG91
B	ARG91
C	ARG91
D	ARG91

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site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:28031352

Chain	Residue	Details
A	HIS124
B	HIS124
C	HIS124
D	HIS124

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site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583

Chain	Residue	Details
A	ASP161
B	ASP161
C	ASP161
D	ASP161

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site_id	SWS_FT_FI6
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:21963988, ECO:0007744|PDB:3MBI

Chain	Residue	Details
A	ARG186
A	ASP210
B	ARG186
B	ASP210
C	ARG186
C	ASP210
D	ARG186
D	ASP210

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