3DAH

2.3 A crystal structure of ribose-phosphate pyrophosphokinase from Burkholderia pseudomallei

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	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	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
C	0000166	molecular_function	nucleotide 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	0009156	biological_process	ribonucleoside monophosphate biosynthetic process
C	0009165	biological_process	nucleotide biosynthetic process
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 319

Chain	Residue
A	ASN50
A	ARG52
A	ARG108
B	SER310
B	MET312

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 319

Chain	Residue
C	ARG52
A	SER310
A	MET312
B	ARG108
C	ASN50

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 320

Chain	Residue
B	ASP226
B	THR227
B	ALA228
B	GLY229
B	THR230

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 320

Chain	Residue
A	ASP226
A	THR227
A	ALA228
A	GLY229
A	THR230

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 319

Chain	Residue
C	ASP226
C	THR227
C	ALA228
C	GLY229
C	THR230

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 B 321

Chain	Residue
B	ARG52
C	ARG108
C	ARG304

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 322

Chain	Residue
B	GLU49
B	ASN50
B	ARG262
C	ARG108

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE AMP A 401

Chain	Residue
A	PHE38
A	ASP40
A	GLU42
A	ARG99
A	GLN100
A	HIS134

---

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP B 401

Chain	Residue
B	PHE38
B	ASP40
B	GLU42
C	ARG99
C	GLN100
C	ARG102
C	PRO104
C	HIS134

---

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE AMP B 402

Chain	Residue
B	ARG99
B	GLN100
B	ARG102
B	HIS134
C	PHE38
C	ASP40
C	GLU42

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS218-THR230

---

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

Chain	Residue	Details
A	ASP132-ASP147

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23382856","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3DAH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23382856","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3DAH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1l1r

Chain	Residue	Details
B	GLY175
B	GLU212

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1l1r

Chain	Residue	Details
C	GLY175
C	GLU212

---