eF-site ID 5d0a-A PDB Code 5d0a Chain A click to enlarge Title Crystal structure of epoxyqueuosine reductase with cleaved RNA stem loop Classification oxidoreductase/RNA Compound Epoxyqueuosine reductase Source (5D0A) Sequence A:  NVYQLKEELIEYAKSIGVDKIGFTTADTFDSLKDRLILQE SLGYLSGFEEPDIEKRVTPKLLLPKAKSIVAIALAYPSRM KDAPRSTRTERRGIFCRASWGKDYHDVLREKLDLLEDFLK SKHDIRTKSMVDTGELSDRAVAERAGIGFSAKNCMITTPE YGSYVYLAEMITNIPFEPDVPIEDMCGSCTKCLDACPTGA LVNPGQLNAQRCISFLTQTKGFLPDEFRTKIGNRLYGCDT CQTVCPLNKGKDFHLHPEMEPDPEIAKPLLKPLLAISNRE FKEKFGHVSGSWRGKKPIQRNAILALAHFKDASALPELTE LMHKDPRPVIRGTAAWAIGKIGDPAYAEELEKALEKEKDE EAKLEIEKGIELLKASGMT Description Functional site 1) chain A residue 153 type sequence A description binding site for residue SF4 A 501 source : AC1 2) chain A residue 154 type sequence K description binding site for residue SF4 A 501 source : AC1 3) chain A residue 155 type sequence N description binding site for residue SF4 A 501 source : AC1 4) chain A residue 188 type sequence C description binding site for residue SF4 A 501 source : AC1 5) chain A residue 191 type sequence C description binding site for residue SF4 A 501 source : AC1 6) chain A residue 194 type sequence C description binding site for residue SF4 A 501 source : AC1 7) chain A residue 247 type sequence C description binding site for residue SF4 A 501 source : AC1 8) chain A residue 249 type sequence L description binding site for residue SF4 A 501 source : AC1 9) chain A residue 198 type sequence C description binding site for residue SF4 A 502 source : AC2 10) chain A residue 199 type sequence P description binding site for residue SF4 A 502 source : AC2 11) chain A residue 209 type sequence L description binding site for residue SF4 A 502 source : AC2 12) chain A residue 214 type sequence C description binding site for residue SF4 A 502 source : AC2 13) chain A residue 215 type sequence I description binding site for residue SF4 A 502 source : AC2 14) chain A residue 240 type sequence C description binding site for residue SF4 A 502 source : AC2 15) chain A residue 242 type sequence T description binding site for residue SF4 A 502 source : AC2 16) chain A residue 243 type sequence C description binding site for residue SF4 A 502 source : AC2 17) chain A residue 32 type sequence S description binding site for residue B12 A 503 source : AC3 18) chain A residue 33 type sequence L description binding site for residue B12 A 503 source : AC3 19) chain A residue 36 type sequence R description binding site for residue B12 A 503 source : AC3 20) chain A residue 47 type sequence S description binding site for residue B12 A 503 source : AC3 21) chain A residue 49 type sequence F description binding site for residue B12 A 503 source : AC3 22) chain A residue 50 type sequence E description binding site for residue B12 A 503 source : AC3 23) chain A residue 57 type sequence R description binding site for residue B12 A 503 source : AC3 24) chain A residue 97 type sequence C description binding site for residue B12 A 503 source : AC3 25) chain A residue 134 type sequence D description binding site for residue B12 A 503 source : AC3 26) chain A residue 138 type sequence L description binding site for residue B12 A 503 source : AC3 27) chain A residue 139 type sequence S description binding site for residue B12 A 503 source : AC3 28) chain A residue 140 type sequence D description binding site for residue B12 A 503 source : AC3 29) chain A residue 141 type sequence R description binding site for residue B12 A 503 source : AC3 30) chain A residue 142 type sequence A description binding site for residue B12 A 503 source : AC3 31) chain A residue 152 type sequence S description binding site for residue B12 A 503 source : AC3 32) chain A residue 155 type sequence N description binding site for residue B12 A 503 source : AC3 33) chain A residue 156 type sequence C description binding site for residue B12 A 503 source : AC3 34) chain A residue 157 type sequence M description binding site for residue B12 A 503 source : AC3 35) chain A residue 158 type sequence I description binding site for residue B12 A 503 source : AC3 36) chain A residue 165 type sequence S description binding site for residue B12 A 503 source : AC3 37) chain A residue 167 type sequence V description binding site for residue B12 A 503 source : AC3 38) chain A residue 169 type sequence L description binding site for residue B12 A 503 source : AC3 39) chain A residue 206 type sequence P description binding site for residue B12 A 503 source : AC3 40) chain A residue 209 type sequence L description binding site for residue B12 A 503 source : AC3 41) chain A residue 216 type sequence S description binding site for residue B12 A 503 source : AC3 42) chain A residue 217 type sequence F description binding site for residue B12 A 503 source : AC3 43) chain A residue 239 type sequence G description binding site for residue B12 A 503 source : AC3 44) chain A residue 240 type sequence C description binding site for residue B12 A 503 source : AC3 45) chain A residue 241 type sequence D description binding site for residue B12 A 503 source : AC3 46) chain A residue 243 type sequence C description binding site for residue B12 A 503 source : AC3 47) chain A residue 244 type sequence Q description binding site for residue B12 A 503 source : AC3 48) chain A residue 49 type sequence F description binding site for residue GOL A 504 source : AC4 49) chain A residue 134 type sequence D description binding site for residue GOL A 504 source : AC4 50) chain A residue 220 type sequence Q description binding site for residue GOL A 504 source : AC4 51) chain A residue 238 type sequence Y description binding site for residue GOL A 504 source : AC4 52) chain A residue 294 type sequence W description binding site for residue GOL A 504 source : AC4 53) chain A residue 112 type sequence K description binding site for residue PO4 A 505 source : AC5 54) chain A residue 258 type sequence H description binding site for residue PO4 A 505 source : AC5 55) chain A residue 259 type sequence P description binding site for residue PO4 A 505 source : AC5 56) chain A residue 260 type sequence E description binding site for residue PO4 A 505 source : AC5 57) chain A residue 188-199 type prosite sequence CGSCTKCLDACP description 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CgSCTkCLdACP source prosite : PS00198 58) chain A residue 220 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 59) chain A residue 222 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 60) chain A residue 280 type BINDING sequence N description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 61) chain A residue 281 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 62) chain A residue 295 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 63) chain A residue 297 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 64) chain A residue 298 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 65) chain A residue 134 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:27638883 source Swiss-Prot : SWS_FT_FI1 66) chain A residue 247 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 67) chain A residue 214 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 68) chain A residue 216 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 69) chain A residue 240 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 70) chain A residue 243 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 71) chain A residue 57 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 72) chain A residue 191 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 73) chain A residue 194 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 74) chain A residue 198 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 75) chain A residue 97 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 76) chain A residue 134 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 77) chain A residue 139 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 78) chain A residue 152 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 79) chain A residue 155 type BINDING sequence N description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 80) chain A residue 158 type BINDING sequence I description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 81) chain A residue 169 type BINDING sequence L description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 82) chain A residue 188 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2

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