Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1Q1G

Crystal structure of Plasmodium falciparum PNP with 5'-methylthio-immucillin-H

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	MTI301
B	ARG45

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 402

Chain	Residue
B	GLY90
B	SER91
B	MTI302
B	HOH780
A	ARG45
B	GLY23
B	ARG88

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 403

Chain	Residue
C	GLY23
C	ARG88
C	GLY90
C	SER91
C	MTI303
C	HOH888
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	GLY90
D	SER91
D	MTI304
D	HOH768

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	MTI305
E	HOH710
F	ARG45

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 F 406

Chain	Residue
E	ARG45
F	GLY23
F	ARG88
F	GLY90
F	SER91
F	MTI306
F	HOH893

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 407

Chain	Residue
B	HIS123
B	GLY124
B	ASP125
B	IPA502
B	HOH681
B	HOH736
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	IPA507
D	HOH841
D	HOH935
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	IPA505
F	HOH836

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 410

Chain	Residue
B	LYS101
B	ARG102

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 F 411

Chain	Residue
F	LYS101
F	ARG102
F	HOH811
F	HOH868

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

Chain	Residue
A	HIS224
D	LYS101
D	ARG102
D	LYS211

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 413

Chain	Residue
A	LYS101
A	ARG102
A	ASP216
A	HOH851
D	GLU227

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

Chain	Residue
A	HIS123
A	GLY124
A	ASP125
A	IPA503
A	HOH834
F	ARG169

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 415

Chain	Residue
D	ARG169
E	HIS123
E	GLY124
E	ASP125
E	IPA506
E	HOH833

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 416

Chain	Residue
B	ARG169
B	IPA508
C	HIS123
C	GLY124
C	ASP125
C	HOH839
C	HOH848

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

Chain	Residue
B	HIS7
B	LYS9
B	ASN44
B	ARG45

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 418

Chain	Residue
A	HIS7
A	LYS9
A	ASN44
A	ARG45
B	ASN219

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 F 419

Chain	Residue
F	HIS7
F	LYS9
F	ASN44
F	ARG45

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 420

Chain	Residue
E	HIS7
E	LYS9
E	ASN44
E	ARG45

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 421

Chain	Residue
C	HOH809
D	HIS7
D	LYS9
D	ASN44
D	ARG45

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 422

Chain	Residue
C	HIS7
C	LYS9
C	ASN44
C	ARG45
D	ASN219

site_id	CC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE MTI A 301

Chain	Residue
A	VAL66
A	ARG88
A	SER91
A	CYS92
A	GLY93
A	TYR160
A	GLU182
A	MET183
A	GLU184
A	ASP206
A	TRP212
A	SO4401
A	HOH690
A	HOH835
A	HOH934
B	HIS7
B	VAL73

site_id	CC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE MTI B 302

Chain	Residue
A	HIS7
A	VAL73
B	VAL66
B	ARG88
B	SER91
B	CYS92
B	GLY93
B	TYR160
B	GLU182
B	MET183
B	GLU184
B	ASP206
B	TRP212
B	SO4402
B	HOH677
B	HOH852
B	HOH854

site_id	CC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MTI 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	HOH650
C	HOH898
C	HOH910
D	HIS7
D	VAL73

site_id	CC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MTI D 304

Chain	Residue
C	HIS7
C	VAL73
D	ARG88
D	SER91
D	CYS92
D	GLY93
D	TYR160
D	GLU182
D	MET183
D	GLU184
D	ASP206
D	TRP212
D	SO4404
D	HOH617
D	HOH829
D	HOH855

site_id	CC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE MTI E 305

Chain	Residue
E	VAL66
E	ARG88
E	SER91
E	CYS92
E	GLY93
E	TYR160
E	GLU182
E	MET183
E	GLU184
E	ASP206
E	TRP212
E	SO4405
E	HOH646
E	HOH923
E	HOH927
F	HIS7
F	VAL73

site_id	DC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MTI F 306

Chain	Residue
E	VAL73
F	ARG88
F	SER91
F	CYS92
F	GLY93
F	TYR160
F	GLU182
F	MET183
F	GLU184
F	ASP206
F	PRO209
F	TRP212
F	SO4406
F	HOH742
F	HOH798
F	HOH832

site_id	DC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA B 501

Chain	Residue
A	ARG169
B	ARG116
B	LEU120
B	HOH865

site_id	DC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA B 502

Chain	Residue
B	HIS119
B	HIS123
B	SO4407
C	ARG169

site_id	DC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA A 503

Chain	Residue
A	HIS119
A	HIS123
A	SO4414
F	ARG169

site_id	DC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA F 504

Chain	Residue
E	ARG169
F	ARG116
F	LEU120
F	HOH846

site_id	DC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA F 505

Chain	Residue
A	ARG169
F	HIS119
F	HIS123
F	SO4409

site_id	DC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA E 506

Chain	Residue
D	ARG169
E	HIS119
E	HIS123
E	SO4415

site_id	DC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA D 507

Chain	Residue
D	HIS119
D	HIS123
D	SO4408
E	ARG169

site_id	DC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA B 508

Chain	Residue
B	ARG169
C	HIS119
C	HIS123
C	SO4416

site_id	EC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA D 509

Chain	Residue
C	ARG169
D	ARG116
D	LEU120
D	HOH908

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)