2XCW

Crystal structure of the D52N variant of cytosolic 5'-nucleotidase II in complex with inosine monophosphate and ATP

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	BINDING SITE FOR RESIDUE ATP A 1489

Chain	Residue
A	ARG144
A	ARG456
A	TYR457
A	GOL1495
A	MG1497
A	MG1497
A	HOH2154
A	HOH2386
A	HOH2387
A	HOH2388
A	HOH2389
A	ASP145
A	HOH2390
A	HOH2390
A	HOH2391
A	HOH2392
A	HOH2393
A	HOH2394
A	HOH2395
A	HOH2396
A	HOH2396
A	HOH2397
A	THR147
A	ILE152
A	ASN154
A	PHE354
A	LYS362
A	GLN453
A	ARG456

---

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE IMP A 1490

Chain	Residue
A	ASN52
A	MET53
A	ASP54
A	PHE157
A	ARG202
A	ASP206
A	HIS209
A	TYR210
A	LYS215
A	THR249
A	ASN250
A	SER251
A	LYS292
A	MG1498
A	HOH2170
A	HOH2214
A	HOH2283
A	HOH2331
A	HOH2332
A	HOH2398
A	HOH2399
A	HOH2400

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 1491

Chain	Residue
A	PHE283
A	ASP284
A	LEU321
A	GLN322
A	HIS323
A	GLY324
A	ILE325
A	HOH2274
A	HOH2401

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1492

Chain	Residue
A	PHE198
A	GLN199
A	ARG202
A	ASP206
A	HOH2402
A	HOH2403

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1493

Chain	Residue
A	PRO96
A	THR97
A	GLU374
A	GLU378
A	TYR434
A	HOH2344
A	HOH2404
A	HOH2405

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1494

Chain	Residue
A	ASP257
A	THR261
A	PRO278
A	TRP279
A	GLN280
A	HOH2240
A	HOH2406

---

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 1495

Chain	Residue
A	TYR151
A	ILE152
A	LEU153
A	ASN154
A	ASN158
A	HIS352
A	ATP1489
A	HOH2407
A	HOH2409

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1496

Chain	Residue
A	ASP252
A	TYR253
A	VAL288
A	ASP289
A	GLY310
A	LEU312

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 1497

Chain	Residue
A	HOH2396
A	ATP1489
A	ATP1489
A	HOH2396

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1498

Chain	Residue
A	ASN52
A	ASP54
A	ASP351
A	IMP1490
A	HOH2331
A	HOH2332

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:21396942

Chain	Residue	Details
A	ASN52

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:21396942

Chain	Residue	Details
A	ASP54

---

site_id	SWS_FT_FI3
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, 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
A	ASN52
A	ASP54

---

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

Chain	Residue	Details
A	ARG144
A	ARG456

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XJC

Chain	Residue	Details
A	ASN154
A	LYS362
A	GLN453
A	TYR457

---

site_id	SWS_FT_FI6
Number of Residues	7
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

---

site_id	SWS_FT_FI7
Number of Residues	1
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

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:17405878, ECO:0007744|PDB:2JC9

Chain	Residue	Details
A	MET436

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER418
A	SER511

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	SER502

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3V1L4

Chain	Residue	Details
A	SER527

---