4Q8V

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

Functional Information from GO Data

Chain	GOid	namespace	contents
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	HOH716
A	HOH827
A	PRO56
A	GLU57
A	GLY94
A	TRP95
A	ASP96

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site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 2YX A 403

Chain	Residue
A	ASP102
A	TYR106
A	ASP156
A	CYS158
A	ILE201
A	GLN203
A	GLY229
A	GLY230
A	LEU231
A	ALA232
A	MET260
A	GLY261
A	CYS281
A	VAL282
A	ARG286
A	HOH799
A	HOH844

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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

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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

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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	ASP102
A	ASP156
A	GLN203
A	GLY230

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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	CYS318
A	CYS320
A	CYS323
A	HIS349

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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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