Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1U9Z

Crystal Structure of Phosphoribosyl Diphosphate Synthase Complexed with AMP and Ribose 5-Phosphate

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	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	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	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
D	0000166	molecular_function	nucleotide 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	0016740	molecular_function	transferase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE R5P A 5301

Chain	Residue
A	ASP163
A	HOH5445
A	ASP212
A	ILE214
A	ILE215
A	SER216
A	THR217
A	GLY218
A	GLY219
A	THR220

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE R5P B 6301

Chain	Residue
B	ASP163
B	ASP212
B	ILE214
B	ILE215
B	SER216
B	THR217
B	GLY218
B	GLY219
B	THR220
B	HOH6445

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE R5P C 7301

Chain	Residue
C	ASP163
C	ASP212
C	ILE214
C	ILE215
C	SER216
C	THR217
C	GLY218
C	GLY219
C	THR220
C	HOH7445

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE R5P D 8301

Chain	Residue
D	ASP163
D	ASP212
D	ILE214
D	SER216
D	THR217
D	GLY218
D	GLY219
D	THR220
D	HOH8445

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AMP B 5302

Chain	Residue
A	ARG92
A	GLN93
A	ASP94
A	PHE97
A	HIS125
B	PHE32
B	ASP34
B	GLU36
B	HOH5424
B	HOH5437

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AMP B 6302

Chain	Residue
A	PHE32
A	ASP34
A	GLU36
B	ARG92
B	GLN93
B	ASP94
B	PHE97
B	HIS125
B	HOH6424
B	HOH6437

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AMP D 7302

Chain	Residue
C	ARG92
C	GLN93
C	PHE97
C	HIS125
D	PHE32
D	ASP34
D	GLU36
D	HOH7424
D	HOH7437

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AMP C 8302

Chain	Residue
C	PHE32
C	ASP34
C	GLU36
C	HOH8424
C	HOH8437
D	ARG92
D	GLN93
D	PHE97
D	HIS125

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16288921","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U9Z","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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":"16288921","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1U9Z","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding 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
A	LYS164
A	ASP202

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

Chain	Residue	Details
B	LYS164
B	ASP202

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1l1r

Chain	Residue	Details
C	LYS164
C	ASP202

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1l1r

Chain	Residue	Details
D	LYS164
D	ASP202

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