eF-site ID 6h62-AB PDB Code 6h62 Chain A, B click to enlarge Title QTRT1, the catalytic subunit of murine tRNA-Guanine Transglycosylase Classification TRANSFERASE Compound Queuine tRNA-ribosyltransferase catalytic subunit 1 Source (TGT_MOUSE) Sequence A:  ESAPRIMRLVAECSRSGARAGELRLPHGTVATPVFMPVGT QATMKGITTEQLDSLGCRICLGNTGLHGFMNWPHNLLTDS GGFQMSEVTEEGVHFRSPYDGEETLLSPERSVEIQNALGS DIIMQLDHVVSSTVTGPLVEEAMHRSVRWLDRCIAAHKHP DKQNLFAIIQGGLNADLRTTCLKEMTKRDVPGFAIGGLSG GESKAQFWKMVALSTSMLPKDKPRYLMGVGYATDLVVCVA LGCDMFDCVYPTRTARFGSALVPTGNLQLKKKQYAKDFSP INPECPCPTCQTHSRAFLHALLHSDNTTALHHLTVHNIAY QLQLLSAVRSSILEQRFPDFVRNFMRTMYGDHSLCPAWAV EALASVGIML B:  SAPRIMRLVAECSRSGARAGELRLPHGTVATPVFMPVGTQ ATMKGITTEQLDSLGCRICLGNGLHGFMNWPHNLLTDSGG FQMSEVTEEGVHFRSPYDGEETLLSPERSVEIQNALGSDI IMQLDHVVSTGPLVEEAMHRSVRWLDRCIAAHKHPDKQNL FAIIQGGLNADLRTTCLKEMTKRDVPGFAIGGLSGGESKA QFWKMVALSTSMLPKDKPRYLMGVGYATDLVVCVALGCDM FDCVYPTRTARFGSALVPTGNLQLKKKQYAKDFSPINPEC PCPTCQTHSRAFLHALLHSDNTTALHHLTVHNIAYQLQLL SAVRSSILEQRFPDFVRNFMRTMYGDHSLCPAWAVEALAS VGIMLT Description Functional site 1) chain A residue 317 type sequence C description binding site for residue ZN A 501 source : AC1 2) chain A residue 319 type sequence C description binding site for residue ZN A 501 source : AC1 3) chain A residue 322 type sequence C description binding site for residue ZN A 501 source : AC1 4) chain A residue 348 type sequence H description binding site for residue ZN A 501 source : AC1 5) chain A residue 355 type sequence Q description binding site for residue GOL A 502 source : AC2 6) chain A residue 359 type sequence A description binding site for residue GOL A 502 source : AC2 7) chain B residue 317 type sequence C description binding site for residue ZN B 501 source : AC3 8) chain B residue 319 type sequence C description binding site for residue ZN B 501 source : AC3 9) chain B residue 322 type sequence C description binding site for residue ZN B 501 source : AC3 10) chain B residue 348 type sequence H description binding site for residue ZN B 501 source : AC3 11) chain B residue 295 type sequence P description binding site for residue GOL B 502 source : AC4 12) chain B residue 355 type sequence Q description binding site for residue GOL B 502 source : AC4 13) chain A residue 139 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9BXR0 source Swiss-Prot : SWS_FT_FI7 14) chain B residue 139 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9BXR0 source Swiss-Prot : SWS_FT_FI7 15) chain A residue 105 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03218 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 105 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03218 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 159 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI4 18) chain A residue 202 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI4 19) chain A residue 229 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI4 20) chain B residue 159 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI4 21) chain B residue 202 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI4 22) chain B residue 229 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI4 23) chain A residue 317 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:6H62, ECO:0007744|PDB:7B2I, ECO:0007744|PDB:7OV9, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OVS, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI5 24) chain A residue 319 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:6H62, ECO:0007744|PDB:7B2I, ECO:0007744|PDB:7OV9, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OVS, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI5 25) chain A residue 322 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:6H62, ECO:0007744|PDB:7B2I, ECO:0007744|PDB:7OV9, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OVS, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI5 26) chain A residue 348 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:6H62, ECO:0007744|PDB:7B2I, ECO:0007744|PDB:7OV9, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OVS, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI5 27) chain B residue 317 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:6H62, ECO:0007744|PDB:7B2I, ECO:0007744|PDB:7OV9, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OVS, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI5 28) chain B residue 319 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:6H62, ECO:0007744|PDB:7B2I, ECO:0007744|PDB:7OV9, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OVS, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI5 29) chain B residue 322 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:6H62, ECO:0007744|PDB:7B2I, ECO:0007744|PDB:7OV9, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OVS, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI5 30) chain B residue 348 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:35815944, ECO:0007744|PDB:6H62, ECO:0007744|PDB:7B2I, ECO:0007744|PDB:7OV9, ECO:0007744|PDB:7OVO, ECO:0007744|PDB:7OVS, ECO:0007744|PDB:7OWZ source Swiss-Prot : SWS_FT_FI5 31) chain A residue 105 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03218 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 105 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03218 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 279 type ACT_SITE sequence D description Nucleophile => ECO:0000255|HAMAP-Rule:MF_03218 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 279 type ACT_SITE sequence D description Nucleophile => ECO:0000255|HAMAP-Rule:MF_03218 source Swiss-Prot : SWS_FT_FI2

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