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4HQV

tRNA-guanine transglycosylase Y106F, C158V, V233G mutant in complex with queuine

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
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 Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AARG97
AHOH619
AHOH668
AHOH670
APRO56
AGLU57
AGLY94
ATRP95
AASP96

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
AALA219
AMET250
APRO252
AHOH774
AHOH796

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
AGLN117
AARG174
APRO252
AASP254
ALYS255
AHOH547
AHOH721

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
ATRP296
AGLU317
ALYS360
APHE373
AARG380
AHOH521
AHOH758

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE QEI A 406
ChainResidue
ASER103
APHE106
AASP156
AVAL158
AILE201
AGLN203
AGLY229
AGLY230
ALEU231
AMET260
AHOH573
AHOH667

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

237992

PDB entries from 2025-06-25

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