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5LPT

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0002099biological_processtRNA wobble guanine modification
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
A0008616biological_processtRNA queuosine(34) biosynthetic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0046872molecular_functionmetal ion binding
B0002099biological_processtRNA wobble guanine modification
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006400biological_processtRNA modification
B0008033biological_processtRNA processing
B0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
B0008616biological_processtRNA queuosine(34) biosynthetic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0046872molecular_functionmetal ion binding
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 Residues21
Detailsbinding site for residue 726 A 402
ChainResidue
ATYR106
AGLN107
AASP156
ACYS158
AGLN203
AGLY229
AGLY230
ALEU231
AALA232
ATYR258
AMET260
AGLY261
AASP280
AVAL282
AHOH543
BHOH556
ALEU68
AGLY69
AASN70
AASP102
ASER103

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 403
ChainResidue
AGLY46
AGLY69
AASN70
ALEU74
AMET93
AHOH505
AHOH585

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BCYS318
BCYS320
BCYS323
BHIS349

site_idAC5
Number of Residues21
Detailsbinding site for residue 726 B 402
ChainResidue
AGLU339
AHOH554
BGLY69
BASN70
BASP102
BSER103
BTYR106
BGLN107
BASP156
BCYS158
BILE201
BGLN203
BGLY229
BGLY230
BLEU231
BALA232
BTYR258
BMET260
BGLY261
BASP280
BHOH512

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL B 403
ChainResidue
BLYS360
BARG380
BHOH525
BHOH526

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL B 404
ChainResidue
BALA20
BARG21
BILE365
BSER366
BGLY368

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

237735

PDB entries from 2025-06-18

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