Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3PHC

Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004731	molecular_function	purine-nucleoside phosphorylase activity
A	0004850	molecular_function	uridine phosphorylase activity
A	0005829	cellular_component	cytosol
A	0006148	biological_process	inosine catabolic process
A	0006166	biological_process	purine ribonucleoside salvage
A	0006195	biological_process	purine nucleotide catabolic process
A	0006218	biological_process	uridine catabolic process
A	0009116	biological_process	nucleoside metabolic process
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity
A	0047975	molecular_function	guanosine phosphorylase activity
B	0003824	molecular_function	catalytic activity
B	0004731	molecular_function	purine-nucleoside phosphorylase activity
B	0004850	molecular_function	uridine phosphorylase activity
B	0005829	cellular_component	cytosol
B	0006148	biological_process	inosine catabolic process
B	0006166	biological_process	purine ribonucleoside salvage
B	0006195	biological_process	purine nucleotide catabolic process
B	0006218	biological_process	uridine catabolic process
B	0009116	biological_process	nucleoside metabolic process
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity
B	0047975	molecular_function	guanosine phosphorylase activity
C	0003824	molecular_function	catalytic activity
C	0004731	molecular_function	purine-nucleoside phosphorylase activity
C	0004850	molecular_function	uridine phosphorylase activity
C	0005829	cellular_component	cytosol
C	0006148	biological_process	inosine catabolic process
C	0006166	biological_process	purine ribonucleoside salvage
C	0006195	biological_process	purine nucleotide catabolic process
C	0006218	biological_process	uridine catabolic process
C	0009116	biological_process	nucleoside metabolic process
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity
C	0047975	molecular_function	guanosine phosphorylase activity
D	0003824	molecular_function	catalytic activity
D	0004731	molecular_function	purine-nucleoside phosphorylase activity
D	0004850	molecular_function	uridine phosphorylase activity
D	0005829	cellular_component	cytosol
D	0006148	biological_process	inosine catabolic process
D	0006166	biological_process	purine ribonucleoside salvage
D	0006195	biological_process	purine nucleotide catabolic process
D	0006218	biological_process	uridine catabolic process
D	0009116	biological_process	nucleoside metabolic process
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity
D	0047975	molecular_function	guanosine phosphorylase activity
E	0003824	molecular_function	catalytic activity
E	0004731	molecular_function	purine-nucleoside phosphorylase activity
E	0004850	molecular_function	uridine phosphorylase activity
E	0005829	cellular_component	cytosol
E	0006148	biological_process	inosine catabolic process
E	0006166	biological_process	purine ribonucleoside salvage
E	0006195	biological_process	purine nucleotide catabolic process
E	0006218	biological_process	uridine catabolic process
E	0009116	biological_process	nucleoside metabolic process
E	0016740	molecular_function	transferase activity
E	0016757	molecular_function	glycosyltransferase activity
E	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity
E	0047975	molecular_function	guanosine phosphorylase activity
F	0003824	molecular_function	catalytic activity
F	0004731	molecular_function	purine-nucleoside phosphorylase activity
F	0004850	molecular_function	uridine phosphorylase activity
F	0005829	cellular_component	cytosol
F	0006148	biological_process	inosine catabolic process
F	0006166	biological_process	purine ribonucleoside salvage
F	0006195	biological_process	purine nucleotide catabolic process
F	0006218	biological_process	uridine catabolic process
F	0009116	biological_process	nucleoside metabolic process
F	0016740	molecular_function	transferase activity
F	0016757	molecular_function	glycosyltransferase activity
F	0017061	molecular_function	S-methyl-5-thioadenosine phosphorylase activity
F	0047975	molecular_function	guanosine phosphorylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K A 275

Chain	Residue
A	GLU46
A	VAL66
B	GLU46
B	VAL66

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 502

Chain	Residue
A	IM5501
B	ARG45
A	GLY23
A	ARG27
A	ARG88
A	GLY90
A	SER91

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE IM5 A 501

Chain	Residue
A	SER91
A	CYS92
A	GLY93
A	TYR160
A	VAL181
A	GLU182
A	MET183
A	GLU184
A	ASP206
A	TRP212
A	HOH281
A	HOH294
A	PO4502
B	HIS7

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 502

Chain	Residue
A	ARG45
B	GLY23
B	ARG27
B	ARG88
B	GLY90
B	SER91
B	IM5501

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE IM5 B 501

Chain	Residue
A	HIS7
B	SER91
B	CYS92
B	GLY93
B	TYR160
B	VAL181
B	GLU182
B	MET183
B	GLU184
B	ASP206
B	TRP212
B	HOH315
B	PO4502

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K C 275

Chain	Residue
C	GLU46
C	VAL66
D	GLU46
D	VAL66
D	HOH291

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 502

Chain	Residue
C	GLY23
C	ARG27
C	ARG88
C	GLY90
C	SER91
C	IM5501
D	ARG45

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE IM5 C 501

Chain	Residue
C	SER91
C	CYS92
C	GLY93
C	TYR160
C	VAL181
C	GLU182
C	MET183
C	GLU184
C	ASP206
C	TRP212
C	HOH297
C	HOH314
C	HOH320
C	PO4502
D	HIS7

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 D 502

Chain	Residue
C	ARG45
D	GLY23
D	ARG27
D	ARG88
D	GLY90
D	SER91
D	IM5501

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE IM5 D 501

Chain	Residue
C	HIS7
D	VAL66
D	SER91
D	CYS92
D	GLY93
D	TYR160
D	VAL181
D	GLU182
D	MET183
D	GLU184
D	ASP206
D	TRP212
D	HOH282
D	HOH284
D	HOH300
D	PO4502

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K E 275

Chain	Residue
F	VAL66
F	HOH292
E	GLU46
E	VAL66
E	HOH293
F	GLU46

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 E 502

Chain	Residue
E	GLY23
E	ARG27
E	ARG88
E	GLY90
E	SER91
E	IM5501
F	ARG45

site_id	BC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE IM5 E 501

Chain	Residue
E	VAL66
E	SER91
E	CYS92
E	GLY93
E	TYR160
E	VAL181
E	GLU182
E	MET183
E	GLU184
E	ASP206
E	TRP212
E	HOH288
E	HOH309
E	HOH339
E	PO4502
F	HIS7
F	HOH304

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 F 502

Chain	Residue
E	ARG45
F	GLY23
F	ARG27
F	ARG88
F	GLY90
F	SER91
F	IM5501

site_id	BC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE IM5 F 501

Chain	Residue
E	HIS7
F	SER91
F	CYS92
F	GLY93
F	TYR160
F	VAL181
F	GLU182
F	MET183
F	GLU184
F	ASP206
F	TRP212
F	HOH287
F	HOH307
F	PO4502

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q8I3X4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8I3X4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"30602534","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZNI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"30602534","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZNC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ZNI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"Q8I3X4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 695

Chain	Residue	Details
A	ARG27	electrostatic stabiliser
A	ARG45	electrostatic stabiliser
A	ARG88	electrostatic stabiliser
A	ASP206	proton acceptor, proton donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 695

Chain	Residue	Details
B	ARG27	electrostatic stabiliser
B	ARG45	electrostatic stabiliser
B	ARG88	electrostatic stabiliser
B	ASP206	proton acceptor, proton donor

site_id	MCSA3
Number of Residues	4
Details	M-CSA 695

Chain	Residue	Details
C	ARG27	electrostatic stabiliser
C	ARG45	electrostatic stabiliser
C	ARG88	electrostatic stabiliser
C	ASP206	proton acceptor, proton donor

site_id	MCSA4
Number of Residues	4
Details	M-CSA 695

Chain	Residue	Details
D	ARG27	electrostatic stabiliser
D	ARG45	electrostatic stabiliser
D	ARG88	electrostatic stabiliser
D	ASP206	proton acceptor, proton donor

site_id	MCSA5
Number of Residues	4
Details	M-CSA 695

Chain	Residue	Details
E	ARG27	electrostatic stabiliser
E	ARG45	electrostatic stabiliser
E	ARG88	electrostatic stabiliser
E	ASP206	proton acceptor, proton donor

site_id	MCSA6
Number of Residues	4
Details	M-CSA 695

Chain	Residue	Details
F	ARG27	electrostatic stabiliser
F	ARG45	electrostatic stabiliser
F	ARG88	electrostatic stabiliser
F	ASP206	proton acceptor, proton donor

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