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5LPQ

tRNA guanine Transglycosylase (TGT) in co-crystallized complex (space group P21) with 6-amino-4-(2-((3aR,4R,6R,6aR)-6-methoxy-2,2-dimethyltetrahydrofuro[3,4-d][1,3]dioxol-4-yl)ethyl)-2-(methylamino)-1H-imidazo[4,5-g]quinazolin-8(7H)-one

Functional Information from GO Data
ChainGOidnamespacecontents
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
A0008616biological_processqueuosine biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0046872molecular_functionmetal ion binding
A0101030biological_processtRNA-guanine transglycosylation
B0006400biological_processtRNA modification
B0008033biological_processtRNA processing
B0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
B0008616biological_processqueuosine biosynthetic process
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0046872molecular_functionmetal ion binding
B0101030biological_processtRNA-guanine transglycosylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
ACYS318
ACYS320
ACYS323
AHIS349

site_idAC2
Number of Residues16
Detailsbinding site for residue 72C A 402
ChainResidue
AASP156
ACYS158
AILE201
AGLN203
AGLY229
AGLY230
ALEU231
AALA232
AMET260
AGLY261
BGLU339
AASN70
AASP102
ASER103
ATYR106
AGLN107

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BCYS318
BCYS320
BCYS323
BHIS349

site_idAC4
Number of Residues15
Detailsbinding site for residue 72C B 402
ChainResidue
AGLU339
BLEU68
BASP102
BTYR106
BGLN107
BASP156
BCYS158
BILE201
BGLN203
BGLY229
BGLY230
BLEU231
BALA232
BMET260
BGLY261

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492
ChainResidueDetails
AASP102
BASP102

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492
ChainResidueDetails
AASP280
BASP280

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:12949492
ChainResidueDetails
AASP102
AASP156
AGLN203
AGLY230
BASP102
BASP156
BGLN203
BGLY230

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: 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
ChainResidueDetails
ACYS318
ACYS320
ACYS323
AHIS349
BCYS318
BCYS320
BCYS323
BHIS349

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 881
ChainResidueDetails
AASP102proton shuttle (general acid/base)
AASP280covalent catalysis
ACYS318metal ligand
ACYS320metal ligand
ACYS323metal ligand
AHIS349metal ligand

site_idMCSA2
Number of Residues6
DetailsM-CSA 881
ChainResidueDetails
BASP102proton shuttle (general acid/base)
BASP280covalent catalysis
BCYS318metal ligand
BCYS320metal ligand
BCYS323metal ligand
BHIS349metal ligand

223532

PDB entries from 2024-08-07

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