5L4Z

Crystal structure of enzyme in purine metabolism

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	10
Details	binding site for residue GOL A 601

Chain	Residue
A	ALA114
A	HOH710
A	TYR115
A	ARG144
A	LYS362
A	SER452
A	ARG456
A	ARG456
A	TYR457
A	HOH706

---

site_id	AC2
Number of Residues	5
Details	binding site for residue GOL A 602

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

---

site_id	AC3
Number of Residues	9
Details	binding site for residue GOL A 603

Chain	Residue
A	PHE283
A	ASP284
A	ILE286
A	GLN322
A	HIS323
A	GLY324
A	ILE325
A	HOH721
A	HOH742

---

site_id	AC4
Number of Residues	7
Details	binding site for residue GOL A 604

Chain	Residue
A	GLU374
A	GLU378
A	TYR434
A	GLY438
A	LEU440
A	HOH734
A	HOH791

---

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL A 605

Chain	Residue
A	ASP54
A	HIS209
A	LYS215
A	SER251
A	TYR255

---

site_id	AC6
Number of Residues	8
Details	binding site for residue GOL A 606

Chain	Residue
A	ARG39
A	TYR115
A	ASN117
A	LYS361
A	ARG367
A	ASP459
A	GOL613
A	HOH755

---

site_id	AC7
Number of Residues	7
Details	binding site for residue GOL A 607

Chain	Residue
A	ASP257
A	THR261
A	PRO278
A	TRP279
A	GLN280
A	HOH712
A	HOH740

---

site_id	AC8
Number of Residues	7
Details	binding site for residue GOL A 608

Chain	Residue
A	VAL35
A	VAL37
A	TYR471
A	TYR475
A	ARG478
A	GOL612
A	HOH714

---

site_id	AC9
Number of Residues	6
Details	binding site for residue GOL A 609

Chain	Residue
A	ASN117
A	LEU118
A	ARG134
A	LYS344
A	ARG446
A	GOL613

---

site_id	AD1
Number of Residues	3
Details	binding site for residue GOL A 610

Chain	Residue
A	TYR151
A	GLN199
A	ARG202

---

site_id	AD2
Number of Residues	2
Details	binding site for residue GOL A 611

Chain	Residue
A	PHE191
A	HOH783

---

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL A 612

Chain	Residue
A	ARG34
A	VAL35
A	PHE36
A	VAL37
A	PRO485
A	GOL608

---

site_id	AD4
Number of Residues	5
Details	binding site for residue GOL A 613

Chain	Residue
A	ARG367
A	GOL606
A	GOL609
A	HOH751
A	HOH793

---

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	ASP52

---

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	ASP52
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

---