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

6FSO

Crystal Structure of TGT in complex with methyl({[5-(pyridin-3-yloxy)furan-2-yl]methyl})amine

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 Residues6
Detailsbinding site for residue PEG A 402
ChainResidue
AHOH611
AARG34
AGLY148
ASER149
AASP150
AASN195

site_idAC3
Number of Residues6
Detailsbinding site for residue PEG A 403
ChainResidue
AARG77
AARG303
AARG336
AGLY368
AHOH567
AHOH580

site_idAC4
Number of Residues6
Detailsbinding site for residue PEG A 404
ChainResidue
APRO249
ALEU251
APRO252
AASP253
AASP254
AHOH664

site_idAC5
Number of Residues4
Detailsbinding site for residue DMS A 405
ChainResidue
AGLY94
ATRP95
AASP96
AHOH741

site_idAC6
Number of Residues3
Detailsbinding site for residue F63 A 406
ChainResidue
AGLU173
AARG177
AGLN213

site_idAC7
Number of Residues4
Detailsbinding site for residue PG4 A 407
ChainResidue
ATRP296
AGLU317
AGLN356
ALYS360

site_idAC8
Number of Residues5
Detailsbinding site for residue ACT A 408
ChainResidue
AVAL282
ATHR285
AARG286
AARG289
AHOH540

site_idAC9
Number of Residues6
Detailsbinding site for residue PGE A 409
ChainResidue
ALEU311
APRO313
ALYS325
ATRP326
ASER327
AHOH546

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

PDB statisticsPDBj update infoContact PDBjnumon