eF-site ID 5d0a-C PDB Code 5d0a Chain C click to enlarge Title Crystal structure of epoxyqueuosine reductase with cleaved RNA stem loop Classification oxidoreductase/RNA Compound Epoxyqueuosine reductase Source (5D0A) Sequence C:  NVYQLKEELIEYAKSIGVDKIGFTTADTFDSLKDRLILQE SLGYLSGFEEPDIEKRVTPKLLLPKAKSIVAIALAYPSRM KDAPRSTRTERRGIFCRASWGKDYHDVLREKLDLLEDFLK SKHDIRTKSMVDTGELSDRAVAERAGIGFSAKNCMITTPE YGSYVYLAEMITNIPFEPDVPIEDMCGSCTKCLDACPTGA LVNPGQLNAQRCISFLTQTKGFLPDEFRTKIGNRLYGCDT CQTVCPLNKGKDFHLHPEMEPDPEIAKPLLKPLLAISNRE FKEKFGHVSGSWRGKKPIQRNAILALAHFKDASALPELTE LMHKDPRPVIRGTAAWAIGKIGDPAYAEELEKALEKEKDE EAKLEIEKGIELLKAS Description Functional site 1) chain C residue 153 type sequence A description binding site for residue SF4 C 501 source : AD2 2) chain C residue 154 type sequence K description binding site for residue SF4 C 501 source : AD2 3) chain C residue 155 type sequence N description binding site for residue SF4 C 501 source : AD2 4) chain C residue 188 type sequence C description binding site for residue SF4 C 501 source : AD2 5) chain C residue 191 type sequence C description binding site for residue SF4 C 501 source : AD2 6) chain C residue 194 type sequence C description binding site for residue SF4 C 501 source : AD2 7) chain C residue 247 type sequence C description binding site for residue SF4 C 501 source : AD2 8) chain C residue 198 type sequence C description binding site for residue SF4 C 502 source : AD3 9) chain C residue 209 type sequence L description binding site for residue SF4 C 502 source : AD3 10) chain C residue 214 type sequence C description binding site for residue SF4 C 502 source : AD3 11) chain C residue 215 type sequence I description binding site for residue SF4 C 502 source : AD3 12) chain C residue 240 type sequence C description binding site for residue SF4 C 502 source : AD3 13) chain C residue 242 type sequence T description binding site for residue SF4 C 502 source : AD3 14) chain C residue 243 type sequence C description binding site for residue SF4 C 502 source : AD3 15) chain C residue 32 type sequence S description binding site for residue B12 C 503 source : AD4 16) chain C residue 33 type sequence L description binding site for residue B12 C 503 source : AD4 17) chain C residue 36 type sequence R description binding site for residue B12 C 503 source : AD4 18) chain C residue 47 type sequence S description binding site for residue B12 C 503 source : AD4 19) chain C residue 49 type sequence F description binding site for residue B12 C 503 source : AD4 20) chain C residue 50 type sequence E description binding site for residue B12 C 503 source : AD4 21) chain C residue 57 type sequence R description binding site for residue B12 C 503 source : AD4 22) chain C residue 97 type sequence C description binding site for residue B12 C 503 source : AD4 23) chain C residue 134 type sequence D description binding site for residue B12 C 503 source : AD4 24) chain C residue 138 type sequence L description binding site for residue B12 C 503 source : AD4 25) chain C residue 139 type sequence S description binding site for residue B12 C 503 source : AD4 26) chain C residue 140 type sequence D description binding site for residue B12 C 503 source : AD4 27) chain C residue 141 type sequence R description binding site for residue B12 C 503 source : AD4 28) chain C residue 145 type sequence E description binding site for residue B12 C 503 source : AD4 29) chain C residue 152 type sequence S description binding site for residue B12 C 503 source : AD4 30) chain C residue 155 type sequence N description binding site for residue B12 C 503 source : AD4 31) chain C residue 156 type sequence C description binding site for residue B12 C 503 source : AD4 32) chain C residue 157 type sequence M description binding site for residue B12 C 503 source : AD4 33) chain C residue 158 type sequence I description binding site for residue B12 C 503 source : AD4 34) chain C residue 165 type sequence S description binding site for residue B12 C 503 source : AD4 35) chain C residue 167 type sequence V description binding site for residue B12 C 503 source : AD4 36) chain C residue 169 type sequence L description binding site for residue B12 C 503 source : AD4 37) chain C residue 206 type sequence P description binding site for residue B12 C 503 source : AD4 38) chain C residue 207 type sequence G description binding site for residue B12 C 503 source : AD4 39) chain C residue 209 type sequence L description binding site for residue B12 C 503 source : AD4 40) chain C residue 216 type sequence S description binding site for residue B12 C 503 source : AD4 41) chain C residue 217 type sequence F description binding site for residue B12 C 503 source : AD4 42) chain C residue 239 type sequence G description binding site for residue B12 C 503 source : AD4 43) chain C residue 240 type sequence C description binding site for residue B12 C 503 source : AD4 44) chain C residue 241 type sequence D description binding site for residue B12 C 503 source : AD4 45) chain C residue 243 type sequence C description binding site for residue B12 C 503 source : AD4 46) chain C residue 244 type sequence Q description binding site for residue B12 C 503 source : AD4 47) chain C residue 49 type sequence F description binding site for residue GOL C 504 source : AD5 48) chain C residue 134 type sequence D description binding site for residue GOL C 504 source : AD5 49) chain C residue 220 type sequence Q description binding site for residue GOL C 504 source : AD5 50) chain C residue 238 type sequence Y description binding site for residue GOL C 504 source : AD5 51) chain C residue 294 type sequence W description binding site for residue GOL C 504 source : AD5 52) chain C residue 112 type sequence K description binding site for residue PO4 C 505 source : AD6 53) chain C residue 258 type sequence H description binding site for residue PO4 C 505 source : AD6 54) chain C residue 259 type sequence P description binding site for residue PO4 C 505 source : AD6 55) chain C residue 260 type sequence E description binding site for residue PO4 C 505 source : AD6 56) chain C residue 134 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:27638883 source Swiss-Prot : SWS_FT_FI1 57) chain C residue 57 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 58) chain C residue 97 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 59) chain C residue 134 type BINDING sequence D description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 60) chain C residue 139 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 61) chain C residue 152 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 62) chain C residue 155 type BINDING sequence N description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 63) chain C residue 158 type BINDING sequence I description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 64) chain C residue 169 type BINDING sequence L description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 65) chain C residue 188 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 66) chain C residue 191 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 67) chain C residue 194 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 68) chain C residue 198 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 69) chain C residue 214 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 70) chain C residue 216 type BINDING sequence S description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 71) chain C residue 240 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 72) chain C residue 243 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 73) chain C residue 247 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B source Swiss-Prot : SWS_FT_FI2 74) chain C residue 220 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 75) chain C residue 222 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 76) chain C residue 280 type BINDING sequence N description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 77) chain C residue 281 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 78) chain C residue 295 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 79) chain C residue 297 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3 80) chain C residue 298 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27638883 source Swiss-Prot : SWS_FT_FI3

Display surface Download Links