eF-site ID 6vww-AB PDB Code 6vww Chain A, B click to enlarge Title Crystal Structure of NSP15 Endoribonuclease from SARS CoV-2. Classification VIRAL PROTEIN Compound Uridylate-specific endoribonuclease Source (R1AB_SARS2) Sequence A:  NMSLENVAFNVVNKGHFDGQQGEVPVSIINNTVYTKVDGV DVELFENKTTLPVNVAFELWAKRNIKPVPEVKILNNLGVD IAANTVIWDYKRDAPAHISTIGVCSMTDIAKKPTETICAP LTVFFDGRVDGQVDLFRNARNGVLITEGSVKGLQPSVGPK QASLNGVTLIGEAVKTQFNYYKKVDGVVQQLPETYFTQSR NLQEFKPRSQMEIDFLELAMDEFIERYKLEGYAFEHIVYG DFSHSQLGGLHLLIGLAKRFKESPFELEDFIPMDSTVKNY FITDAQTGSSKCVCSVIDLLLDDFVEIIKSQDLSVVSKVV KVTIDYTEISFMLWCKDGHVETFYPKLQ B:  NMSLENVAFNVVNKGHFDGQQGEVPVSIINNTVYTKVDGV DVELFENKTTLPVNVAFELWAKRNIKPVPEVKILNNLGVD IAANTVIWDYKRDAPAHISTIGVCSMTDIAKKPTETICAP LTVFFDGRVDGQVDLFRNARNGVLITEGSVKGLQPSVGPK QASLNGVTLIGEAVKTQFNYYKKVDGVVQQLPETYFTQSR NLQEFKPRSQMEIDFLELAMDEFIERYKLEGYAFEHIVYG DFSHSQLGGLHLLIGLAKRFKESPFELEDFIPMDSTVKNY FITDAQTGSSKCVCSVIDLLLDDFVEIIKSQDLSVVSKVV KVTIDYTEISFMLWCKDGHVETFYPKLQ Description Functional site 1) chain A residue 43 type sequence L description binding site for residue GOL A 401 source : AC1 2) chain A residue 44 type sequence F description binding site for residue GOL A 401 source : AC1 3) chain A residue 45 type sequence E description binding site for residue GOL A 401 source : AC1 4) chain A residue 267 type sequence E description binding site for residue GOL A 401 source : AC1 5) chain A residue 126 type sequence G description binding site for residue GOL A 402 source : AC2 6) chain A residue 127 type sequence R description binding site for residue GOL A 402 source : AC2 7) chain A residue 145 type sequence T description binding site for residue GOL A 402 source : AC2 8) chain A residue 146 type sequence E description binding site for residue GOL A 402 source : AC2 9) chain A residue 147 type sequence G description binding site for residue GOL A 402 source : AC2 10) chain A residue 262 type sequence S description binding site for residue MG A 403 source : AC3 11) chain A residue 263 type sequence P description binding site for residue MG A 403 source : AC3 12) chain A residue 283 type sequence D description binding site for residue MG A 403 source : AC3 13) chain A residue 284 type sequence A description binding site for residue MG A 403 source : AC3 14) chain A residue 285 type sequence Q description binding site for residue MG A 403 source : AC3 15) chain A residue 77 type sequence G description binding site for residue GOL A 404 source : AC4 16) chain A residue 79 type sequence D description binding site for residue GOL A 404 source : AC4 17) chain A residue 119 type sequence P description binding site for residue GOL A 404 source : AC4 18) chain A residue 69 type sequence E description binding site for residue GOL A 405 source : AC5 19) chain A residue 90 type sequence K description binding site for residue GOL A 405 source : AC5 20) chain A residue 167 type sequence T description binding site for residue GOL A 405 source : AC5 21) chain A residue 198 type sequence S description binding site for residue GOL A 405 source : AC5 22) chain A residue 200 type sequence N description binding site for residue GOL A 405 source : AC5 23) chain A residue 200 type sequence N description binding site for residue ACY A 406 source : AC6 24) chain A residue 201 type sequence L description binding site for residue ACY A 406 source : AC6 25) chain A residue 279 type sequence Y description binding site for residue ACY A 406 source : AC6 26) chain B residue 75 type sequence N description binding site for residue GOL B 401 source : AC7 27) chain B residue 274 type sequence S description binding site for residue GOL B 401 source : AC7 28) chain B residue 275 type sequence T description binding site for residue GOL B 401 source : AC7 29) chain B residue 276 type sequence V description binding site for residue GOL B 401 source : AC7 30) chain B residue 90 type sequence K description binding site for residue GOL B 402 source : AC8 31) chain B residue 167 type sequence T description binding site for residue GOL B 402 source : AC8 32) chain B residue 198 type sequence S description binding site for residue GOL B 402 source : AC8 33) chain B residue 199 type sequence R description binding site for residue GOL B 402 source : AC8 34) chain B residue 200 type sequence N description binding site for residue GOL B 402 source : AC8 35) chain B residue 77 type sequence G description binding site for residue GOL B 403 source : AC9 36) chain B residue 79 type sequence D description binding site for residue GOL B 403 source : AC9 37) chain B residue 119 type sequence P description binding site for residue GOL B 403 source : AC9 38) chain B residue 121 type sequence T description binding site for residue GOL B 403 source : AC9 39) chain A residue 322 type sequence T description binding site for residue CL B 404 source : AD1 40) chain B residue 149 type sequence V description binding site for residue CL B 404 source : AD1 41) chain B residue 151 type sequence G description binding site for residue CL B 404 source : AD1 42) chain B residue 43 type sequence L description binding site for residue GOL B 405 source : AD2 43) chain B residue 44 type sequence F description binding site for residue GOL B 405 source : AD2 44) chain B residue 45 type sequence E description binding site for residue GOL B 405 source : AD2 45) chain B residue 59 type sequence W description binding site for residue GOL B 405 source : AD2 46) chain B residue 192 type sequence E description binding site for residue GOL B 406 source : AD3 47) chain B residue 320 type sequence K description binding site for residue GOL B 406 source : AD3 48) chain B residue 322 type sequence T description binding site for residue GOL B 406 source : AD3 49) chain B residue 327 type sequence E description binding site for residue GOL B 406 source : AD3 50) chain B residue 146 type sequence E description binding site for residue ACY B 407 source : AD4 51) chain B residue 174 type sequence K description binding site for residue ACY B 407 source : AD4 52) chain B residue 176 type sequence Q description binding site for residue ACY B 407 source : AD4 53) chain B residue 177 type sequence F description binding site for residue ACY B 407 source : AD4 54) chain B residue 178 type sequence N description binding site for residue ACY B 407 source : AD4 55) chain B residue 312 type sequence L description binding site for residue ACY B 408 source : AD5 56) chain B residue 313 type sequence S description binding site for residue ACY B 408 source : AD5 57) chain B residue 314 type sequence V description binding site for residue ACY B 408 source : AD5 58) chain B residue 315 type sequence V description binding site for residue ACY B 408 source : AD5 59) chain B residue 334 type sequence C description binding site for residue ACY B 408 source : AD5 60) chain B residue 335 type sequence K description binding site for residue ACY B 408 source : AD5 61) chain B residue 336 type sequence D description binding site for residue ACY B 408 source : AD5 62) chain B residue 337 type sequence G description binding site for residue ACY B 408 source : AD5 63) chain A residue 290 type BINDING sequence K description BINDING => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI4 64) chain B residue 290 type BINDING sequence K description BINDING => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI4 65) chain A residue 235 type ACT_SITE sequence H description Proton donor; for uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI1 66) chain B residue 235 type ACT_SITE sequence H description Proton donor; for uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI1 67) chain A residue 250 type ACT_SITE sequence H description Proton acceptor; for uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI2 68) chain B residue 250 type ACT_SITE sequence H description Proton acceptor; for uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI2 69) chain A residue 290 type ACT_SITE sequence K description For uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779 source Swiss-Prot : SWS_FT_FI3 70) chain B residue 290 type ACT_SITE sequence K description For uridylate-specific endoribonuclease nsp15 activity => ECO:0000269|PubMed:33504779 source Swiss-Prot : SWS_FT_FI3 71) chain A residue 341 type BINDING sequence T description BINDING => ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI5 72) chain B residue 341 type BINDING sequence T description BINDING => ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI5 73) chain A residue 290 type SITE sequence K description Transition state stabilizer => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI6 74) chain B residue 290 type SITE sequence K description Transition state stabilizer => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI6 75) chain A residue 294 type SITE sequence S description Uracil recognition site => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI7 76) chain B residue 294 type SITE sequence S description Uracil recognition site => ECO:0000269|PubMed:33504779, ECO:0000269|PubMed:33564093 source Swiss-Prot : SWS_FT_FI7 77) chain A residue 347 type SITE sequence Q description Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 source Swiss-Prot : SWS_FT_FI8 78) chain B residue 347 type SITE sequence Q description Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 source Swiss-Prot : SWS_FT_FI8

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