Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1NW4

Crystal Structure of Plasmodium falciparum Purine Nucleoside Phosphorylase in complex with ImmH and Sulfate

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	6
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	GLY23
A	ARG88
A	GLY90
A	SER91
A	IMH301
B	ARG45

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 402

Chain	Residue
B	GLY90
B	SER91
B	IMH302
A	ARG45
B	GLY23
B	ARG88

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 403

Chain	Residue
C	GLY23
C	ARG88
C	GLY90
C	SER91
C	IMH303
D	ARG45

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 404

Chain	Residue
C	ARG45
D	GLY23
D	ARG88
D	ALA89
D	GLY90
D	SER91
D	IMH304

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 E 405

Chain	Residue
E	GLY23
E	ARG88
E	GLY90
E	SER91
E	IMH305
E	HOH833
F	ARG45

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 406

Chain	Residue
E	ARG45
F	GLY23
F	ARG88
F	GLY90
F	SER91
F	IMH306

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 407

Chain	Residue
B	GLY124
B	ASP125
B	IPA508
B	HOH813
C	ARG169

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 408

Chain	Residue
D	HIS123
D	GLY124
D	ASP125
D	IPA514
D	HOH686
D	HOH787
E	ARG169

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 409

Chain	Residue
A	ARG169
F	HIS123
F	GLY124
F	ASP125
F	IPA512
F	HOH643

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 410

Chain	Residue
B	LYS101
B	ARG102
B	ASP216

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 411

Chain	Residue
A	ASP218
A	ASN219
A	ASN220

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 412

Chain	Residue
A	LYS101
A	ARG102
A	ASP216
D	PRO223

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 413

Chain	Residue
A	HIS123
A	GLY124
A	ASP125
A	IPA510
A	HOH601
F	ARG169

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 414

Chain	Residue
F	LYS101
F	ARG102
F	ASP216
F	HOH739
F	HOH803
F	HOH816

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 F 415

Chain	Residue
F	ARG27
F	ASN220
F	LEU221

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 416

Chain	Residue
D	ARG169
E	HIS123
E	GLY124
E	ASP125
E	IPA513
E	HOH806

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 417

Chain	Residue
A	HIS224
D	LYS101
D	ARG102
D	ASP216

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 418

Chain	Residue
B	ARG169
B	IPA515
C	HIS123
C	GLY124
C	ASP125
C	HOH694

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 419

Chain	Residue
E	ASP216
E	LYS101
E	ARG102

site_id	CC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE IMH A 301

Chain	Residue
A	ARG88
A	SER91
A	CYS92
A	GLY93
A	TYR160
A	GLU182
A	MET183
A	GLU184
A	ASP206
A	TRP212
A	SO4401
A	HOH613
A	HOH637
A	HOH647
B	HIS7
B	IPA501

site_id	CC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE IMH B 302

Chain	Residue
A	HIS7
A	IPA502
B	ARG88
B	SER91
B	CYS92
B	GLY93
B	TYR160
B	GLU182
B	MET183
B	GLU184
B	ASP206
B	TRP212
B	SO4402
B	HOH764

site_id	CC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE IMH C 303

Chain	Residue
C	ARG88
C	SER91
C	CYS92
C	GLY93
C	TYR160
C	GLU182
C	MET183
C	GLU184
C	ASP206
C	TRP212
C	SO4403
C	HOH720
C	HOH838
D	HIS7
D	IPA503

site_id	CC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE IMH D 304

Chain	Residue
C	HIS7
D	ARG88
D	SER91
D	CYS92
D	GLY93
D	TYR160
D	VAL181
D	GLU182
D	MET183
D	GLU184
D	ASP206
D	TRP212
D	SO4404
D	HOH662
D	HOH675
D	HOH676

site_id	CC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE IMH E 305

Chain	Residue
E	ARG88
E	SER91
E	CYS92
E	GLY93
E	TYR160
E	GLU182
E	MET183
E	GLU184
E	ASP206
E	TRP212
E	SO4405
E	HOH728
E	HOH772
E	HOH788
F	HIS7

site_id	CC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE IMH F 306

Chain	Residue
E	HIS7
F	ARG88
F	SER91
F	CYS92
F	GLY93
F	GLU182
F	MET183
F	GLU184
F	ASP206
F	TRP212
F	SO4406
F	HOH605
F	HOH693
F	HOH767
F	HOH832

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA B 501

Chain	Residue
A	IMH301
B	ASN44
B	ARG45
B	HOH839
B	HOH840

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA A 502

Chain	Residue
A	ARG6
A	ASN44
A	ARG45
B	IMH302

site_id	DC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IPA D 503

Chain	Residue
C	IMH303
D	ARG6
D	ARG45

site_id	DC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA C 504

Chain	Residue
C	ARG6
C	ASN44
C	ARG45
D	HOH675

site_id	DC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IPA F 505

Chain	Residue
E	HOH772
F	ASN44
F	ARG45

site_id	DC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IPA E 506

Chain	Residue
E	ASN44
E	ARG45
F	HOH767

site_id	DC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IPA B 507

Chain	Residue
A	ARG169
B	ARG116
B	HIS119

site_id	DC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA B 508

Chain	Residue
B	HIS119
B	HIS123
B	SO4407
C	ARG169

site_id	DC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA A 509

Chain	Residue
A	ARG116
A	HIS119
A	HOH822
B	ARG169

site_id	DC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA A 510

Chain	Residue
A	HIS119
A	HIS123
A	SO4413
F	ARG169

site_id	DC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA F 511

Chain	Residue
E	ARG169
F	ARG116
F	HIS119
F	LEU120
F	HOH618

site_id	EC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA F 512

Chain	Residue
A	ARG169
F	HIS119
F	HIS123
F	SO4409

site_id	EC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA E 513

Chain	Residue
D	ARG169
E	HIS119
E	HIS123
E	SO4416

site_id	EC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA D 514

Chain	Residue
D	HIS119
D	HIS123
D	SO4408
E	ARG169

site_id	EC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA B 515

Chain	Residue
B	ARG169
C	HIS119
C	HIS123
C	SO4418

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG.","authors":["Ho M.","Edwards A.A.","Almo S.C.","Schramm V.L."]}},{"source":"PDB","id":"3FOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG.","authors":["Ho M.","Edwards A.A.","Almo S.C.","Schramm V.L."]}},{"source":"PubMed","id":"14982926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19575810","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NW4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ENZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG.","authors":["Ho M.","Edwards A.A.","Almo S.C.","Schramm V.L."]}},{"source":"PubMed","id":"14982926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19575810","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NW4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ENZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	18
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29440412","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG.","authors":["Ho M.","Edwards A.A.","Almo S.C.","Schramm V.L."]}},{"source":"PubMed","id":"14982926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19575810","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NW4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ENZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6AQS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6AQU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"16131758","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG.","authors":["Ho M.","Edwards A.A.","Almo S.C.","Schramm V.L."]}},{"source":"PDB","id":"2BSX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHC","evidenceCode":"ECO:0007744"}]}

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)