eF-site ID 5d0a-B PDB Code 5d0a Chain B click to enlarge Title Crystal structure of epoxyqueuosine reductase with cleaved RNA stem loop Classification oxidoreductase/RNA Compound Epoxyqueuosine reductase Source (5D0A) Sequence B:  NVYQLKEELIEYAKSIGVDKIGFTTADTFDSLKDRLILQE SLGYLSGFEEPDIEKRVTPKLLLPKAKSIVAIALAYPSRM KDAPRSTRTERRGIFCRASWGKDYHDVLREKLDLLEDFLK SKHDIRTKSMVDTGELSDRAVAERAGIGFSAKNCMITTPE YGSYVYLAEMITNIPFEPDVPIEDMCGSCTKCLDACPTGA LVNPGQLNAQRCISFLTQTKGFLPDEFRTKIGNRLYGCDT CQTVCPLNKGKDFHLHPEMEPDPEIAKPLLKPLLAISNRE FKEKFGHVSGSWRGKKPIQRNAILALAHFKDASALPELTE LMHKDPRPVIRGTAAWAIGKIGDPAYAEELEKALEKEKDE EAKLEIEKGIELLKASGMT Description Functional site 1) chain B residue 153 type sequence A description binding site for residue SF4 B 501 source : AC6 2) chain B residue 154 type sequence K description binding site for residue SF4 B 501 source : AC6 3) chain B residue 155 type sequence N description binding site for residue SF4 B 501 source : AC6 4) chain B residue 188 type sequence C description binding site for residue SF4 B 501 source : AC6 5) chain B residue 191 type sequence C description binding site for residue SF4 B 501 source : AC6 6) chain B residue 194 type sequence C description binding site for residue SF4 B 501 source : AC6 7) chain B residue 247 type sequence C description binding site for residue SF4 B 501 source : AC6 8) chain B residue 198 type sequence C description binding site for residue SF4 B 502 source : AC7 9) chain B residue 203 type sequence L description binding site for residue SF4 B 502 source : AC7 10) chain B residue 209 type sequence L description binding site for residue SF4 B 502 source : AC7 11) chain B residue 214 type sequence C description binding site for residue SF4 B 502 source : AC7 12) chain B residue 215 type sequence I description binding site for residue SF4 B 502 source : AC7 13) chain B residue 240 type sequence C description binding site for residue SF4 B 502 source : AC7 14) chain B residue 242 type sequence T description binding site for residue SF4 B 502 source : AC7 15) chain B residue 243 type sequence C description binding site for residue SF4 B 502 source : AC7 16) chain B residue 32 type sequence S description binding site for residue B12 B 503 source : AC8 17) chain B residue 33 type sequence L description binding site for residue B12 B 503 source : AC8 18) chain B residue 36 type sequence R description binding site for residue B12 B 503 source : AC8 19) chain B residue 47 type sequence S description binding site for residue B12 B 503 source : AC8 20) chain B residue 50 type sequence E description binding site for residue B12 B 503 source : AC8 21) chain B residue 57 type sequence R description binding site for residue B12 B 503 source : AC8 22) chain B residue 97 type sequence C description binding site for residue B12 B 503 source : AC8 23) chain B residue 134 type sequence D description binding site for residue B12 B 503 source : AC8 24) chain B residue 138 type sequence L description binding site for residue B12 B 503 source : AC8 25) chain B residue 139 type sequence S description binding site for residue B12 B 503 source : AC8 26) chain B residue 140 type sequence D description binding site for residue B12 B 503 source : AC8 27) chain B residue 141 type sequence R description binding site for residue B12 B 503 source : AC8 28) chain B residue 152 type sequence S description binding site for residue B12 B 503 source : AC8 29) chain B residue 155 type sequence N description binding site for residue B12 B 503 source : AC8 30) chain B residue 156 type sequence C description binding site for residue B12 B 503 source : AC8 31) chain B residue 157 type sequence M description binding site for residue B12 B 503 source : AC8 32) chain B residue 158 type sequence I description binding site for residue B12 B 503 source : AC8 33) chain B residue 165 type sequence S description binding site for residue B12 B 503 source : AC8 34) chain B residue 167 type sequence V description binding site for residue B12 B 503 source : AC8 35) chain B residue 169 type sequence L description binding site for residue B12 B 503 source : AC8 36) chain B residue 206 type sequence P description binding site for residue B12 B 503 source : AC8 37) chain B residue 207 type sequence G description binding site for residue B12 B 503 source : AC8 38) chain B residue 209 type sequence L description binding site for residue B12 B 503 source : AC8 39) chain B residue 216 type sequence S description binding site for residue B12 B 503 source : AC8 40) chain B residue 239 type sequence G description binding site for residue B12 B 503 source : AC8 41) chain B residue 240 type sequence C description binding site for residue B12 B 503 source : AC8 42) chain B residue 241 type sequence D description binding site for residue B12 B 503 source : AC8 43) chain B residue 243 type sequence C description binding site for residue B12 B 503 source : AC8 44) chain B residue 244 type sequence Q description binding site for residue B12 B 503 source : AC8 45) chain B residue 134 type sequence D description binding site for residue GOL B 504 source : AC9 46) chain B residue 220 type sequence Q description binding site for residue GOL B 504 source : AC9 47) chain B residue 238 type sequence Y description binding site for residue GOL B 504 source : AC9 48) chain B residue 294 type sequence W description binding site for residue GOL B 504 source : AC9 49) chain B residue 112 type sequence K description binding site for residue PO4 B 505 source : AD1 50) chain B residue 258 type sequence H description binding site for residue PO4 B 505 source : AD1 51) chain B residue 259 type sequence P description binding site for residue PO4 B 505 source : AD1 52) chain B residue 260 type sequence E description binding site for residue PO4 B 505 source : AD1 53) chain B residue 134 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:27638883 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 57 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 55) chain B residue 97 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 56) chain B residue 134 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 57) chain B residue 139 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 58) chain B residue 152 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 59) chain B residue 155 type BINDING sequence N description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 60) chain B residue 158 type BINDING sequence I description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 61) chain B residue 169 type BINDING sequence L description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 62) chain B residue 188 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 63) chain B residue 191 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 64) chain B residue 194 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 65) chain B residue 198 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 66) chain B residue 214 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 67) chain B residue 216 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 68) chain B residue 240 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 69) chain B residue 243 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 70) chain B residue 247 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 71) chain B residue 280 type BINDING sequence N description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 72) chain B residue 281 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 73) chain B residue 295 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 74) chain B residue 297 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 75) chain B residue 298 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 76) chain B residue 220 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 77) chain B residue 222 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3

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