Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6DDO

Crystal structure of the single mutant (D52N) of the full-length NT5C2 in the basal state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000255	biological_process	allantoin metabolic process
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	0046085	biological_process	adenosine metabolic process
A	0046872	molecular_function	metal ion binding
A	0050146	molecular_function	nucleoside phosphotransferase activity
A	0050483	molecular_function	IMP 5'-nucleotidase activity
A	0050484	molecular_function	GMP 5'-nucleotidase 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
A	0106411	molecular_function	XMP 5'-nucleosidase activity
B	0000255	biological_process	allantoin metabolic process
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	0046085	biological_process	adenosine metabolic process
B	0046872	molecular_function	metal ion binding
B	0050146	molecular_function	nucleoside phosphotransferase activity
B	0050483	molecular_function	IMP 5'-nucleotidase activity
B	0050484	molecular_function	GMP 5'-nucleotidase 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
B	0106411	molecular_function	XMP 5'-nucleosidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue PO4 A 601

Chain	Residue
A	ARG34
A	VAL35
A	VAL37
A	TYR471
A	TYR475
A	PHE477
A	HOH722
A	HOH778

site_id	AC2
Number of Residues	7
Details	binding site for residue PO4 A 602

Chain	Residue
A	MET53
A	ASP54
A	THR249
A	ASN250
A	SER251
A	LYS292
A	ASN52

site_id	AC3
Number of Residues	7
Details	binding site for residue PO4 B 601

Chain	Residue
B	ARG34
B	VAL35
B	VAL37
B	TYR471
B	TYR475
B	PHE477
B	HOH739

site_id	AC4
Number of Residues	7
Details	binding site for residue PO4 B 602

Chain	Residue
B	ASN52
B	MET53
B	ASP54
B	THR249
B	ASN250
B	SER251
B	LYS292

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000305\|PubMed:21396942

Chain	Residue	Details
A	ASN52
B	ASN52

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000305\|PubMed:21396942

Chain	Residue	Details
A	ASP54
B	ASP54

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:17405878, ECO:0000269\|PubMed:21396942, ECO:0007744\|PDB:2J2C, ECO:0007744\|PDB:2JC9, ECO:0007744\|PDB:2JCM, ECO:0007744\|PDB:2XCV, ECO:0007744\|PDB:2XCW, ECO:0007744\|PDB:2XJB, ECO:0007744\|PDB:2XJC, ECO:0007744\|PDB:2XJD, ECO:0007744\|PDB:2XJE

Chain	Residue	Details
B	ASN52
B	ASP54
A	ASN52
A	ASP54

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:21396942, ECO:0007744\|PDB:2XJB

Chain	Residue	Details
B	ARG144
B	ARG456
A	ARG144
A	ARG456

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:21396942, ECO:0007744\|PDB:2XJC

Chain	Residue	Details
A	GLN453
A	TYR457
B	ASN154
B	LYS362
B	GLN453
B	TYR457
A	ASN154
A	LYS362

site_id	SWS_FT_FI6
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269\|PubMed:21396942, ECO:0007744\|PDB:2XCV, ECO:0007744\|PDB:2XCW

Chain	Residue	Details
A	ARG202
A	ASP206
A	LYS215
A	THR249
A	ASN250
A	SER251
A	LYS292
B	ARG202
B	ASP206
B	LYS215
B	THR249
B	ASN250
B	SER251
B	LYS292

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:17405878, ECO:0000269\|PubMed:21396942, ECO:0007744\|PDB:2J2C, ECO:0007744\|PDB:2JC9, ECO:0007744\|PDB:2JCM

Chain	Residue	Details
A	ASP351
B	ASP351

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:17405878, ECO:0007744\|PDB:2JC9

Chain	Residue	Details
A	MET436
B	MET436

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
B	SER418
B	SER511
A	SER418
A	SER511

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	SER502
B	SER502

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q3V1L4

Chain	Residue	Details
A	SER527
B	SER527

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