4Q8U

tRNA-Guanine Transglycosylase (TGT) in Complex with Methyl 4-[2-({6-amino-8-oxo-1H,7H,8H-imidazo[4,5-g]quinazolin-2-yl}amino)ethyl]benzoate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002099	biological_process	tRNA wobble guanine modification
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006400	biological_process	tRNA modification
A	0008033	biological_process	tRNA processing
A	0008479	molecular_function	tRNA-guanosine(34) queuine transglycosylase activity
A	0008616	biological_process	queuosine biosynthetic process
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0046872	molecular_function	metal ion binding
A	0101030	biological_process	tRNA-guanine transglycosylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	CYS318
A	CYS320
A	CYS323
A	HIS349

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 402

Chain	Residue
A	ARG97
A	LYS325
A	HOH748
A	HOH754
A	PRO56
A	GLU57
A	GLY94
A	TRP95
A	ASP96

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 403

Chain	Residue
A	PHE16
A	SER17
A	ILE18
A	GLU119
A	ASP254

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site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 404

Chain	Residue
A	ALA61
A	THR62
A	CYS320
A	ALA321
A	GLU348
A	HOH544
A	HOH703

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 405

Chain	Residue
A	LEU311
A	CYS323
A	SER327
A	HOH595

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 406

Chain	Residue
A	ARG11
A	MET32
A	LYS33
A	ARG34
A	GLY35
A	VAL36
A	HOH725

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 407

Chain	Residue
A	TRP296
A	GLU317
A	LYS360
A	PHE373
A	HOH542
A	HOH709
A	HOH758

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 408

Chain	Residue
A	ARG38
A	ARG60
A	GLY63
A	HOH659

---

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 2YW A 409

Chain	Residue
A	ASP102
A	TYR106
A	ASP156
A	CYS158
A	ILE201
A	GLN203
A	GLY229
A	GLY230
A	LEU231
A	ALA232
A	GLY234
A	MET260
A	GLY261
A	HOH564

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492

Chain	Residue	Details
A	ASP102

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492

Chain	Residue	Details
A	ASP280

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:12949492

Chain	Residue	Details
A	GLY230
A	ASP102
A	ASP156
A	GLN203

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905, ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024, ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492, ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989, ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936

Chain	Residue	Details
A	CYS320
A	CYS323
A	HIS349
A	CYS318

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 881

Chain	Residue	Details
A	ASP102	proton shuttle (general acid/base)
A	ASP280	covalent catalysis
A	CYS318	metal ligand
A	CYS320	metal ligand
A	CYS323	metal ligand
A	HIS349	metal ligand

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