Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5IU6

Crystal structure of E.coli purine nucleoside phosphorylase with 7-deazahypoxanthine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004731	molecular_function	purine-nucleoside phosphorylase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006152	biological_process	purine nucleoside catabolic process
A	0006974	biological_process	DNA damage response
A	0009116	biological_process	nucleoside metabolic process
A	0009164	biological_process	nucleoside catabolic process
A	0016020	cellular_component	membrane
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0019686	biological_process	purine nucleoside interconversion
A	0042278	biological_process	purine nucleoside metabolic process
A	0042802	molecular_function	identical protein binding
A	0047975	molecular_function	guanosine phosphorylase activity
B	0003824	molecular_function	catalytic activity
B	0004731	molecular_function	purine-nucleoside phosphorylase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006152	biological_process	purine nucleoside catabolic process
B	0006974	biological_process	DNA damage response
B	0009116	biological_process	nucleoside metabolic process
B	0009164	biological_process	nucleoside catabolic process
B	0016020	cellular_component	membrane
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0019686	biological_process	purine nucleoside interconversion
B	0042278	biological_process	purine nucleoside metabolic process
B	0042802	molecular_function	identical protein binding
B	0047975	molecular_function	guanosine phosphorylase activity
C	0003824	molecular_function	catalytic activity
C	0004731	molecular_function	purine-nucleoside phosphorylase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006152	biological_process	purine nucleoside catabolic process
C	0006974	biological_process	DNA damage response
C	0009116	biological_process	nucleoside metabolic process
C	0009164	biological_process	nucleoside catabolic process
C	0016020	cellular_component	membrane
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0016763	molecular_function	pentosyltransferase activity
C	0019686	biological_process	purine nucleoside interconversion
C	0042278	biological_process	purine nucleoside metabolic process
C	0042802	molecular_function	identical protein binding
C	0047975	molecular_function	guanosine phosphorylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue 7HX A 301

Chain	Residue
A	CYS91
A	GLY92
A	PHE159
A	VAL178
A	GLU179
A	MET180
A	SER203
A	ASP204

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

Chain	Residue
A	ARG24
A	ARG43
A	ARG87
A	GLY89
A	SER90
A	GLY20

site_id	AC3
Number of Residues	6
Details	binding site for residue 7HX B 301

Chain	Residue
B	GLY92
B	PHE159
B	VAL178
B	GLU179
B	MET180
B	ILE206

site_id	AC4
Number of Residues	7
Details	binding site for residue SO4 B 302

Chain	Residue
B	GLY20
B	ARG87
B	GLY89
B	SER90
B	HOH412
B	HOH418
C	ARG43

site_id	AC5
Number of Residues	8
Details	binding site for residue 7HX C 301

Chain	Residue
C	SER90
C	CYS91
C	GLY92
C	PHE159
C	VAL178
C	GLU179
C	MET180
C	ASP204

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

Chain	Residue
B	ARG43
C	GLY20
C	ARG87
C	GLY89
C	SER90
C	HOH404

Functional Information from PROSITE/UniProt

site_id	PS01232
Number of Residues	16
Details	PNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiPScSIytkEL

Chain	Residue	Details
A	GLY61-LEU76

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4TS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	15
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"11786017","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21672603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OOE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OOH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OPV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11786017","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21672603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OOE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OOH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OPV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	9
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4TS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21672603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 375

Chain	Residue	Details
A	GLY20	electrostatic stabiliser
A	ARG24	electrostatic stabiliser
A	ARG43	electrostatic stabiliser
A	ARG87	electrostatic stabiliser
A	SER90	electrostatic stabiliser
A	ASP204	proton shuttle (general acid/base)
A	ARG217	enhance reactivity

site_id	MCSA2
Number of Residues	7
Details	M-CSA 375

Chain	Residue	Details
B	GLY20	electrostatic stabiliser
B	ARG24	electrostatic stabiliser
B	ARG43	electrostatic stabiliser
B	ARG87	electrostatic stabiliser
B	SER90	electrostatic stabiliser
B	ASP204	proton shuttle (general acid/base)
B	ARG217	enhance reactivity

site_id	MCSA3
Number of Residues	7
Details	M-CSA 375

Chain	Residue	Details
C	GLY20	electrostatic stabiliser
C	ARG24	electrostatic stabiliser
C	ARG43	electrostatic stabiliser
C	ARG87	electrostatic stabiliser
C	SER90	electrostatic stabiliser
C	ASP204	proton shuttle (general acid/base)
C	ARG217	enhance reactivity

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