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2OKO

Z. mobilis tRNA guanine transglycosylase E235Q mutant apo-structure at pH 5.5

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
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 Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 700
ChainResidue
AARG336
AALA20
AARG21
AARG82
ASER308
AHIS332

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
AALA19
ATHR27
AGLY28
ATHR29
ASER366
AGOL712
AHOH1072
AHOH1108
AHOH1122
AHOH1148
AHOH1167

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 702
ChainResidue
APRO56
AGLU57
AGLY94
ATRP95
AASP96
AARG97
AHOH1179
AHOH1209
AHOH1272

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
AASN70
AASP102
AGLN107
AGLY261
AASP280
AHOH1160

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 704
ChainResidue
AGLN117
AARG174
APRO252
AASP254
ALYS255
AHOH1051

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 705
ChainResidue
AARG34
AHIS145
AGLY148
ASER149
AGLU191
AGLN192
AGOL708
AHOH1022
AHOH1079

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 706
ChainResidue
AGLU317
ALYS360
APHE373
AARG380
AHOH1025
AHOH1201

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 707
ChainResidue
AMET172
AGLU173
AMET176
AARG177
AALA217
AGOL715
AHOH1172
AHOH1181

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 708
ChainResidue
AARG34
AGLY87
AGLY88
AGLY148
AGOL705
AHOH1046
AHOH1090

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 709
ChainResidue
AGLU81
AGLU138
AARG139
AGLU142
AHOH1141
AHOH1154
AHOH1217
AHOH1316

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 711
ChainResidue
ACYS158
AGLY229
AGLY230
ALEU231
AALA232
AHOH1202

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 712
ChainResidue
AALA19
AASN304
AALA305
AARG306
ASER366
AGOL701
AHOH1148

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 713
ChainResidue
AHOH1004
AHOH1106

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 715
ChainResidue
AGOL707
AHOH1188
AMET176
AARG177
AALA217
AILE221

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 716
ChainResidue
AGLU22
ALYS24
AGLU273
APHE370
ASER371

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 717
ChainResidue
APRO249
AMET250
ALEU251
APRO252
AASP253
AHOH1276

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
ASER103

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492
ChainResidueDetails
ACYS281

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:12949492
ChainResidueDetails
ASER103
AGLU157
AGLY204
ALEU231

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
AHIS319
AALA321
AGLN324
AASN350

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
ASER103proton shuttle (general acid/base)
ACYS281covalent catalysis
AHIS319metal ligand
AALA321metal ligand
AGLN324metal ligand
AASN350metal ligand

227344

PDB entries from 2024-11-13

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