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

4Q8M

tRNA-Guanine Transglycosylase (TGT) Mutant V262T Apo Structure

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 Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AHOH548
AHOH629
AGLN117
AARG174
APRO252
AASP254
ALYS255

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
ATHR27
AGLY28
ATHR29
ATHR39
AARG362
ASER366
AHOH597
AHOH617
AHOH777

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
APRO56
AGLU57
AGLY94
ATRP95
AASP96
AARG97
AHOH658
AHOH674

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
AALA61
ACYS320
AALA321
AGLU348

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 406
ChainResidue
AGLU317
APHE373
APHE377
AHOH533
AHOH677

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 407
ChainResidue
APHE14
ASER15
APHE16
AGLU119
AARG174
AASP254
ALYS255
AHOH574
AHOH589
AHOH608

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 408
ChainResidue
AGLY229
AGLY230
ALEU231
AVAL233
AHOH765

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 409
ChainResidue
AALA20
AARG21
AARG82
ASER308
AHIS332

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

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon