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2Z1X

tRNA guanine transglycosylase E235Q mutant in complex with preQ1

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 500
ChainResidue
ACYS318
ACYS320
ACYS323
AHIS349

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PRF A 600
ChainResidue
AILE201
AGLN203
AGLY229
AGLY230
ALEU231
AALA232
AMET260
AGOL703
AHOH868
AASP102
ASER103
ATYR106
AASP156
ACYS158

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
AALA19
ATHR27
AGLY28
ATHR29
AARG362
ASER366
AHOH786
AHOH804
AHOH847
AHOH877

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 702
ChainResidue
APRO56
AGLU57
AGLY94
ATRP95
AASP96
AARG97
AHOH774

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
AASP102
AGLY261
AASP280
APRF600
AHOH738

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 705
ChainResidue
AARG34
AHIS145
AGLY148
ASER149
AGLU191
AGLN192
AHOH785
AHOH830

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 710
ChainResidue
AALA61
ATHR62
AHIS319
ACYS320
AALA352
AGLN356

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 712
ChainResidue
AALA19
AASN304
AALA305
AARG306
AHOH847

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 714
ChainResidue
APHE16
ASER17
AILE18
AGLU119
AARG174
AASP254

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 716
ChainResidue
AGLU22
AGLU273
APHE370
ASER371
AHOH850
AHOH878

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_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pud
ChainResidueDetails
AASP102

site_idMCSA1
Number of Residues6
DetailsM-CSA 881
ChainResidueDetails
AASP102proton shuttle (general acid/base)
AASP280covalent catalysis
ACYS318metal ligand
ACYS320metal ligand
ACYS323metal ligand
AHIS349metal ligand

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PDB entries from 2024-10-09

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