eF-site ID 5b2s-ABCD PDB Code 5b2s Chain A, B, C, D click to enlarge Title Crystal structure of the Streptococcus pyogenes Cas9 EQR variant in complex with sgRNA and target DNA (TGAG PAM) Classification HYDROLASE/RNA/DNA Compound Guide RNA Source Streptococcus pyogenes serotype M1 (5B2S) Sequence A:  GGAAAUUAGGUGCGCUUGGCGUUUUAGAGCUAGAAAUAGC AAGUUAAAAUAAGGCUAGUCCGUUAUCAACUUGAAAAAGU G B:  KYSIGLAIGTNSVGWAVITDEYKVPSKKFKVLGNTDRHSI KKNLIGALLFDSGETAEATRLKRTARRRYTRRKNRILYLQ EIFSNEMAKVDDSFFHRLEESFLVEEDKKHERHPIFGNIV DEVAYHEKYPTIYHLRKKLVDSTDKADLRLIYLALAHMIK FRGHFLIEGDLNPDNLFIQLVQTYNQLFEENPINASGVDA KAILSARLSKSRRLENLIAQLPGEKKNGLFGNLIALSLGL TPNFKSNFDLAEDAKLQLSKDTYDDDLDNLLAQIGDQYAD LFLAAKNLSDAILLSDILRVNTEITKAPLSASMIKRYDEH HQDLTLLKALVRQQLPEKYKEIFFDQSKNGYAGYIDGGAS QEEFYKFIKPILEKMDGTEELLVKLNREDLLRKQRTFDNG SIPHQIHLGELHAILRRQEDFYPFLKDNREKIEKILTFRI PYYVGPLARGNSRFAWMTRKSEETITPWNFEEVVDKGASA QSFIERMTNFDKNLPNEKVLPKHSLLYEYFTVYNELTKVK YVTEGMRKPAFLSGEQKKAIVDLLFKTNRKVTVKQLKEDY FKKIEEFDSVEISGVEDRFNASLGTYHDLLKIIKDKDFLD NEENEDILEDIVLTLTLFEDREMIEERLKTYAHLFDDKVM KQLKRRRYTGWGRLSRKLINGIRDKQSGKTILDFLKSDGF ANRNFMQLIHDDSLTFKEDIQKAQDSLHEHIANLAGSPAI KKGILQTVKVVDELVKVMGRHKPENIVIEMARNSRERMKR IEEGIKELGSQILKEHPVENTQLQNEKLYLYYLQNGRDMY VDQELDINRLSDYDVDAIVPQSFLKDDSIDNKVLTRSDKN RGKSDNVPSEEVVKKMKNYWRQLLNAKLITQRKFDNLTKA ERGGLSELDKAGFIKRQLVETRQITKHVAQILDSRMNTKY DENDKLIREVKVITLKSKLVSDFRKDFQFYKVREINNYHH AHDAYLNAVVGTALIKKYPKLESEFVYGKATAKYFFYSNI MNFFKTEITLANGEIRKRPLIETNGETGEIVWDKGRDFAT VRKVLSMPQVNIVKKTEVQTGGFSKESILPKRNSDKLIAR KKDWDPKKYGGFESPTVAYSVLVVAKVEKGKSKKLKSVKE LLGITIMERSSFEKNPIDFLEAKGYKEVKKDLIIKLPKYS LFELENGRKRMLASAGELQKGNELALPSKYVNFLYLASHY EPEDNEQKQLFVEQHKHYLDEIIEQISEFSKRVILADANL DKVLSAYNKHRDKPIREQAENIIHLFTLTNLGAPAAFKYF DTTIDRKQYRSTKEVLDATLIHQSITGLYETRIDLSQLG C:  CAATCTCAGCCAAGCGCACCTAATTTCC D:  TGAGATTG Description Functional site 1) chain A residue 65 type sequence A description binding site for residue K A 101 source : AC1 2) chain A residue 66 type sequence U description binding site for residue K A 101 source : AC1 3) chain B residue 1102 type sequence T description binding site for residue K A 101 source : AC1 4) chain A residue 68 type sequence A description binding site for residue K A 102 source : AC2 5) chain B residue 1350 type sequence Q description binding site for residue K A 102 source : AC2 6) chain A residue 21 type sequence G description binding site for residue K A 103 source : AC3 7) chain A residue 50 type sequence U description binding site for residue MG A 104 source : AC4 8) chain A residue 63 type sequence U description binding site for residue EDO A 106 source : AC6 9) chain A residue 64 type sequence U description binding site for residue EDO A 106 source : AC6 10) chain B residue 461 type sequence R description binding site for residue EDO A 106 source : AC6 11) chain A residue 66 type sequence U description binding site for residue ACT A 107 source : AC7 12) chain A residue 67 type sequence C description binding site for residue ACT A 107 source : AC7 13) chain B residue 1102 type sequence T description binding site for residue ACT A 107 source : AC7 14) chain B residue 1171 type sequence R description binding site for residue ACT A 107 source : AC7 15) chain B residue 623 type sequence L description binding site for residue K B 1401 source : AC8 16) chain B residue 624 type sequence T description binding site for residue K B 1401 source : AC8 17) chain B residue 626 type sequence F description binding site for residue K B 1401 source : AC8 18) chain B residue 656 type sequence Y description binding site for residue K B 1401 source : AC8 19) chain B residue 584 type sequence E description binding site for residue K B 1402 source : AC9 20) chain B residue 586 type sequence R description binding site for residue K B 1402 source : AC9 21) chain B residue 588 type sequence N description binding site for residue K B 1402 source : AC9 22) chain B residue 226 type sequence I description binding site for residue K B 1403 source : AD1 23) chain B residue 229 type sequence L description binding site for residue K B 1403 source : AD1 24) chain B residue 232 type sequence E description binding site for residue K B 1403 source : AD1 25) chain B residue 361 type sequence G description binding site for residue K B 1404 source : AD2 26) chain B residue 362 type sequence Y description binding site for residue K B 1404 source : AD2 27) chain B residue 365 type sequence G description binding site for residue K B 1404 source : AD2 28) chain B residue 367 type sequence A description binding site for residue K B 1404 source : AD2 29) chain A residue 22 type sequence U description binding site for residue K B 1405 source : AD3 30) chain B residue 364 type sequence D description binding site for residue K B 1405 source : AD3 31) chain B residue 365 type sequence G description binding site for residue K B 1405 source : AD3 32) chain B residue 108 type sequence E description binding site for residue K B 1406 source : AD4 33) chain B residue 109 type sequence E description binding site for residue K B 1406 source : AD4 34) chain B residue 111 type sequence K description binding site for residue K B 1406 source : AD4 35) chain B residue 57 type sequence E description binding site for residue K B 1407 source : AD5 36) chain B residue 576 type sequence D description binding site for residue K B 1408 source : AD6 37) chain B residue 577 type sequence S description binding site for residue K B 1408 source : AD6 38) chain B residue 640 type sequence A description binding site for residue K B 1408 source : AD6 39) chain B residue 643 type sequence F description binding site for residue K B 1408 source : AD6 40) chain A residue 52 type sequence A description binding site for residue EDO B 1410 source : AD8 41) chain B residue 1105 type sequence F description binding site for residue EDO B 1410 source : AD8 42) chain B residue 1168 type sequence I description binding site for residue EDO B 1410 source : AD8 43) chain B residue 1169 type sequence M description binding site for residue EDO B 1410 source : AD8 44) chain B residue 1171 type sequence R description binding site for residue EDO B 1410 source : AD8 45) chain B residue 1172 type sequence S description binding site for residue EDO B 1410 source : AD8 46) chain B residue 1139 type sequence V description binding site for residue EDO B 1411 source : AD9 47) chain B residue 1165 type sequence G description binding site for residue EDO B 1411 source : AD9 48) chain B residue 1167 type sequence T description binding site for residue EDO B 1411 source : AD9 49) chain A residue 19 type sequence G description binding site for residue EDO B 1412 source : AE1 50) chain A residue 20 type sequence C description binding site for residue EDO B 1412 source : AE1 51) chain B residue 136 type sequence Y description binding site for residue EDO B 1412 source : AE1 52) chain B residue 139 type sequence R description binding site for residue EDO B 1412 source : AE1 53) chain B residue 160 type sequence H description binding site for residue EDO B 1412 source : AE1 54) chain B residue 407 type sequence N description binding site for residue EDO B 1412 source : AE1 55) chain B residue 415 type sequence H description binding site for residue EDO B 1412 source : AE1 56) chain B residue 10 type ACT_SITE sequence A description For RuvC-like nuclease domain => ECO:0000305|PubMed:24529477 source Swiss-Prot : SWS_FT_FI1 57) chain B residue 840 type ACT_SITE sequence A description Proton acceptor for HNH nuclease domain => ECO:0000305|PubMed:24529477 source Swiss-Prot : SWS_FT_FI2 58) chain B residue 10 type BINDING sequence A description BINDING => ECO:0000269|PubMed:24505130 source Swiss-Prot : SWS_FT_FI3 59) chain B residue 762 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24505130 source Swiss-Prot : SWS_FT_FI3 60) chain B residue 983 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24505130 source Swiss-Prot : SWS_FT_FI3 61) chain B residue 1297 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24505130 source Swiss-Prot : SWS_FT_FI3 62) chain B residue 1328 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24505130 source Swiss-Prot : SWS_FT_FI3

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