7NQ4

Human tRNA guanine transglycosylase (TGT), RNA-bound covalent intermediate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005741	cellular_component	mitochondrial outer membrane
A	0006400	biological_process	tRNA modification
A	0008033	biological_process	tRNA processing
A	0008479	molecular_function	tRNA-guanosine(34) queuine transglycosylase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0032991	cellular_component	protein-containing complex
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0046982	molecular_function	protein heterodimerization activity
A	0101030	biological_process	tRNA-guanine transglycosylation
A	0120507	cellular_component	tRNA-guanine transglycosylase complex
A	1990234	cellular_component	transferase complex
B	0000049	molecular_function	tRNA binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005741	cellular_component	mitochondrial outer membrane
B	0006400	biological_process	tRNA modification
B	0008033	biological_process	tRNA processing
B	0008479	molecular_function	tRNA-guanosine(34) queuine transglycosylase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0046982	molecular_function	protein heterodimerization activity
B	0101030	biological_process	tRNA-guanine transglycosylation
B	0120507	cellular_component	tRNA-guanine transglycosylase complex
B	1990234	cellular_component	transferase complex

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:34241577, ECO:0007744|PDB:7NQ4

Chain	Residue	Details
B	CYS351
B	CYS353
B	CYS356
B	HIS382

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_03218

Chain	Residue	Details
A	ASP279

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:30149595, ECO:0000269|PubMed:34241577, ECO:0007744|PDB:6H45, ECO:0007744|PDB:7NQ4

Chain	Residue	Details
A	ASP105
A	ASP159
A	GLY229
A	CYS317
A	CYS319
A	CYS322
A	HIS348

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:34241577, ECO:0007744|PDB:7NQ4

Chain	Residue	Details
A	GLN202

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22814378

Chain	Residue	Details
A	ALA2

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER139

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