Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5JT5

tRNA guanine Transglycosylase (TGT) in co-crystallized complex with 2-((2-morpholinoethyl)amino)-1H-benzo[d]imidazole-5-carboxamide

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 401
ChainResidue
ACYS318
ACYS320
ACYS323
AHIS349

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 402
ChainResidue
AARG97
ALYS325
AHOH568
AHOH753
APRO56
AGLU57
AGLY94
ATRP95
AASP96

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 403
ChainResidue
AGLU317
ALYS360
APHE373
AARG380
AHOH550
AHOH677
AHOH688

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 404
ChainResidue
ALEU311
APRO313
ACYS323
AGLN324
ALYS325
ATRP326
AHOH503

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 405
ChainResidue
ATHR285
AARG289
AHOH521

site_idAC6
Number of Residues12
Detailsbinding site for residue 6NK A 406
ChainResidue
ATYR106
AASP156
ACYS158
AGLN203
AGLY229
AGLY230
ALEU231
AALA232
AMET260
AGLY261
AHOH564
AHOH765

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO A 407
ChainResidue
AHIS145
AGLY148
ASER149
AGLN192
AHOH545
AHOH604

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

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon