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5I02

tRNA guanine transglycosylase (TGT) in co-crystallized complex with 6-amino-4-{2-[(cyclohexylmethyl)amino]ethyl}-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one

Functional Information from GO Data
ChainGOidnamespacecontents
A0002099biological_processtRNA wobble guanine modification
A0005829cellular_componentcytosol
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
A0008616biological_processqueuosine biosynthetic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0046872molecular_functionmetal ion binding
A0101030biological_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 Residues18
Detailsbinding site for residue PK2 A 402
ChainResidue
AASP156
ACYS158
AILE201
AGLN203
AGLY229
AGLY230
ALEU231
AALA232
AMET260
AGLY261
AASP280
AVAL282
AHOH643
AGLY69
AASN70
AASP102
ASER103
ATYR106

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 403
ChainResidue
ATHR27
AGLY28
AARG38
AARG362
ASER366
AEDO404

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 404
ChainResidue
AASN304
AGLN359
AASP363
ASER366
AEDO403
AHOH519

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO A 405
ChainResidue
AHIS145
ALEU146
ASER188
AARG189
ALYS190
AGLU191
AHOH653

site_idAC6
Number of Residues8
Detailsbinding site for residue GOL A 406
ChainResidue
AGLN117
ASER118
AARG174
APRO252
AASP254
ALYS255
AHOH529
AHOH686

site_idAC7
Number of Residues8
Detailsbinding site for residue GOL A 407
ChainResidue
AARG34
AHIS145
AGLY148
ASER149
AGLU191
AGLN192
AHOH501
AHOH549

site_idAC8
Number of Residues4
Detailsbinding site for residue CL A 408
ChainResidue
ATYR72
AGLY104
AGLN107
AHOH658

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492
ChainResidueDetails
AASP102

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492
ChainResidueDetails
AASP280

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:12949492
ChainResidueDetails
AASP102
AASP156
AGLN203
AGLY230

site_idSWS_FT_FI4
Number of Residues4
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

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

218853

PDB entries from 2024-04-24

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