1DKU

CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0002189	cellular_component	ribose phosphate diphosphokinase complex
A	0003824	molecular_function	catalytic activity
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	0009156	biological_process	ribonucleoside monophosphate biosynthetic process
A	0009165	biological_process	nucleotide biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0002189	cellular_component	ribose phosphate diphosphokinase complex
B	0003824	molecular_function	catalytic activity
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	0009156	biological_process	ribonucleoside monophosphate biosynthetic process
B	0009165	biological_process	nucleotide biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AP2 B 1001

Chain	Residue
A	LYS105
B	VAL311
B	SER312
B	PHE315
B	HOH1005
B	HOH1006
B	HOH1029
A	SER108
A	ARG109
B	SER52
B	ARG54
B	GLN140
B	ASP148
B	HIS149
B	SER310

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE AP2 A 1002

Chain	Residue
A	SER52
A	ARG54
A	GLN140
A	ASP148
A	HIS149
A	SER310
A	VAL311
A	SER312
A	PHE315
A	HOH1010
B	LYS105
B	ALA106
B	ARG107
B	SER108
B	ARG109
B	HOH1045

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ABM A 1003

Chain	Residue
A	ARG101
A	GLN102
A	ALA106
A	HIS135
A	HOH1046
A	HOH1096
A	HOH1097
A	HOH1098
B	PHE40
B	ASP42
B	GLU44

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ABM B 1004

Chain	Residue
A	PHE40
A	ASP42
A	GLU44
B	ARG101
B	GLN102
B	ARG104
B	ALA106
B	GLU110
B	HIS135
B	HOH1088

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA219-THR231

---

site_id	PS00114
Number of Residues	16
Details	PRPP_SYNTHASE Phosphoribosyl pyrophosphate synthase signature. DLHApQIQGFFdiPID

Chain	Residue	Details
A	ASP133-ASP148

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"28031352","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16008562","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10742175","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11790837","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10742175","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1DKU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IBS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10742175","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1DKU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28031352","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"11790837","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1IBS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q97CA5","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10742175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11790837","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DKR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IBS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
A	ASP224
A	ASP223
A	ASP227
A	CYS250

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
B	ASP224
B	ASP223
B	ASP227
B	CYS250

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