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2NQZ

Trna-guanine transglycosylase (TGT) mutant in complex with 7-deaza-7-aminomethyl-guanine

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_processqueuosine biosynthetic process
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 400
ChainResidue
ACYS318
ACYS320
ACYS323
AHIS349

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PRF A 500
ChainResidue
AGLN203
AGLY229
AGLY230
ALEU231
ASER232
AMET260
AGOL704
AHOH1175
AHOH1185
AHOH1282
ASER103
APHE106
AASP156
AVAL158
AILE201

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 700
ChainResidue
AALA19
ATHR27
AGLY28
ATHR39
AARG362
ASER366
AHOH1206
AHOH1345

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
APRO56
AGLU57
AGLY94
ATRP95
AASP96
AARG97

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 702
ChainResidue
AGLN117
ASER118
AARG174
APRO252
AASP254
ALYS255
AHOH1161

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
AHIS145
AGLY148
ASER149
AGLN192
AHOH1174
AHOH1178

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 704
ChainResidue
AVAL45
AASN70
AASP102
AGLN107
AGLY261
AASP280
APRF500
AHOH1216
AHOH1306
AHOH1308
AHOH1358

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 705
ChainResidue
AALA20
AARG21
AARG82
ASER308
AHIS332
AARG336
AHOH1311
AHOH1350

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
ASER103

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492
ChainResidueDetails
ACYS281

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:12949492
ChainResidueDetails
ASER103
AGLU157
AGLY204
ALEU231

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
AHIS319
AALA321
AGLN324
AASN350

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pud
ChainResidueDetails
AASP102

site_idMCSA1
Number of Residues6
DetailsM-CSA 881
ChainResidueDetails
ASER103proton shuttle (general acid/base)
ACYS281covalent catalysis
AHIS319metal ligand
AALA321metal ligand
AGLN324metal ligand
AASN350metal ligand

226707

PDB entries from 2024-10-30

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