Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5CR7

Human cytosolic 5'-nucleotidase II in complex with N-(9H-Purin-6-yl)-3-(3-pyrrol-1-ylphenyl)benzamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000255	biological_process	allantoin metabolic process
A	0003824	molecular_function	catalytic activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006204	biological_process	IMP catabolic process
A	0008253	molecular_function	5'-nucleotidase activity
A	0009117	biological_process	nucleotide metabolic process
A	0016740	molecular_function	transferase activity
A	0016787	molecular_function	hydrolase activity
A	0042802	molecular_function	identical protein binding
A	0046037	biological_process	GMP metabolic process
A	0046040	biological_process	IMP metabolic process
A	0046054	biological_process	dGMP metabolic process
A	0046055	biological_process	dGMP catabolic process
A	0046085	biological_process	adenosine metabolic process
A	0046872	molecular_function	metal ion binding
A	0050146	molecular_function	nucleoside phosphotransferase activity
A	0050689	biological_process	negative regulation of defense response to virus by host
A	0061630	molecular_function	ubiquitin protein ligase activity
A	0070936	biological_process	protein K48-linked ubiquitination
B	0000166	molecular_function	nucleotide binding
B	0000255	biological_process	allantoin metabolic process
B	0003824	molecular_function	catalytic activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006204	biological_process	IMP catabolic process
B	0008253	molecular_function	5'-nucleotidase activity
B	0009117	biological_process	nucleotide metabolic process
B	0016740	molecular_function	transferase activity
B	0016787	molecular_function	hydrolase activity
B	0042802	molecular_function	identical protein binding
B	0046037	biological_process	GMP metabolic process
B	0046040	biological_process	IMP metabolic process
B	0046054	biological_process	dGMP metabolic process
B	0046055	biological_process	dGMP catabolic process
B	0046085	biological_process	adenosine metabolic process
B	0046872	molecular_function	metal ion binding
B	0050146	molecular_function	nucleoside phosphotransferase activity
B	0050689	biological_process	negative regulation of defense response to virus by host
B	0061630	molecular_function	ubiquitin protein ligase activity
B	0070936	biological_process	protein K48-linked ubiquitination

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue 5WO A 601

Chain	Residue
A	LEU57
A	VAL59
A	LYS231
A	SER464
A	ILE466
A	HOH702
A	HOH721
A	HOH774

site_id	AC2
Number of Residues	3
Details	binding site for residue ACT A 602

Chain	Residue
A	GLU241
A	GLY243
A	LYS240

site_id	AC3
Number of Residues	4
Details	binding site for residue ACT A 603

Chain	Residue
A	GLY130
A	ARG134
A	LYS140
B	LYS344

site_id	AC4
Number of Residues	1
Details	binding site for residue ACT A 604

Chain	Residue
A	TYR91

site_id	AC5
Number of Residues	4
Details	binding site for residue ACT A 605

Chain	Residue
A	GLU487
A	SER488
A	GLU491
A	HIS492

site_id	AC6
Number of Residues	3
Details	binding site for residue ACT A 606

Chain	Residue
A	TYR253
A	ASP289
A	GLY310

site_id	AC7
Number of Residues	6
Details	binding site for residue ACT A 607

Chain	Residue
A	LYS26
A	ARG28
A	ARG34
A	ARG478
A	PO4609
A	HOH730

site_id	AC8
Number of Residues	10
Details	binding site for residue PO4 A 608

Chain	Residue
A	ASP52
A	MET53
A	ASP54
A	THR249
A	ASN250
A	SER251
A	LYS292
A	MG610
A	GOL614
A	HOH709

site_id	AC9
Number of Residues	9
Details	binding site for residue PO4 A 609

Chain	Residue
A	ARG34
A	VAL35
A	VAL37
A	TYR471
A	TYR475
A	PHE477
A	ACT607
A	HOH712
A	HOH730

site_id	AD1
Number of Residues	5
Details	binding site for residue MG A 610

Chain	Residue
A	ASP52
A	ASP54
A	ASP351
A	PO4608
A	HOH739

site_id	AD2
Number of Residues	1
Details	binding site for residue GOL A 611

Chain	Residue
A	TRP366

site_id	AD3
Number of Residues	1
Details	binding site for residue GOL A 612

Chain	Residue
A	ARG238

site_id	AD4
Number of Residues	2
Details	binding site for residue GOL A 613

Chain	Residue
A	TYR55
A	GLU374

site_id	AD5
Number of Residues	5
Details	binding site for residue GOL A 614

Chain	Residue
A	PHE157
A	HIS209
A	ASN250
A	SER251
A	PO4608

site_id	AD6
Number of Residues	2
Details	binding site for residue GOL A 617

Chain	Residue
A	GLU220
A	ASN221

site_id	AD7
Number of Residues	2
Details	binding site for residue GOL A 618

Chain	Residue
A	LYS61
A	GLU223

site_id	AD8
Number of Residues	5
Details	binding site for residue 5WO B 601

Chain	Residue
B	VAL59
B	VAL227
B	SER464
B	ILE466
B	HOH702

site_id	AD9
Number of Residues	4
Details	binding site for residue ACT B 602

Chain	Residue
B	PRO293
B	HIS352
B	PHE354
B	GLY355

site_id	AE1
Number of Residues	2
Details	binding site for residue ACT B 603

Chain	Residue
B	LYS240
B	GLU241

site_id	AE2
Number of Residues	4
Details	binding site for residue ACT B 604

Chain	Residue
B	GLU487
B	VAL490
B	GLU491
B	HIS492

site_id	AE3
Number of Residues	2
Details	binding site for residue ACT B 605

Chain	Residue
B	TYR91
B	ASP92

site_id	AE4
Number of Residues	8
Details	binding site for residue PO4 B 606

Chain	Residue
B	ASP52
B	MET53
B	ASP54
B	THR249
B	ASN250
B	SER251
B	LYS292
B	MG609

site_id	AE5
Number of Residues	6
Details	binding site for residue PO4 B 607

Chain	Residue
B	ARG34
B	VAL35
B	VAL37
B	TYR471
B	TYR475
B	PHE477

site_id	AE6
Number of Residues	3
Details	binding site for residue PO4 B 608

Chain	Residue
B	LYS215
B	PHE157
B	HIS209

site_id	AE7
Number of Residues	4
Details	binding site for residue MG B 609

Chain	Residue
B	ASP52
B	ASP54
B	ASP351
B	PO4606

site_id	AE8
Number of Residues	3
Details	binding site for residue GOL B 610

Chain	Residue
B	ILE80
B	ASP187
B	MET192

site_id	AE9
Number of Residues	4
Details	binding site for residue GOL B 611

Chain	Residue
A	HIS481
B	PHE389
B	MET430
B	GLY444

site_id	AF1
Number of Residues	3
Details	binding site for residue GOL B 612

Chain	Residue
B	PHE296
B	GLY365
B	TRP366

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17405878","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J2C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JC9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JCM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XCV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XCW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XJB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XJC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XJD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XJE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XJB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XJC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XCV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XCW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17405878","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J2C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JC9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JCM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17405878","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JC9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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