eF-site ID 2r6d-ABCDEF PDB Code 2r6d Chain A, B, C, D, E, F click to enlarge Title Crystal Form B1 Classification REPLICATION Compound Replicative helicase Source Geobacillus stearothermophilus (Bacillus stearothermophilus) (Q9X4C9_BACST) Sequence A:  PPQSIEAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQ KIFHAMLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYL SELADAVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDG YTREDEIDVLLDEADRKIMEVSQRAFKNIKDILVQTYDNI EMLHNRDGEITGIPTGFTELDRMTSGFQRSDLIIVAARPS VGKTAFALNIAQNVATKTNENVAIFSLEMSAQQLVMRMLC AEGNINAQNLRTGKLTPEDWGKLTMAMGSLSNAGIYIDDT PSIRVSDIRAKCRRLKQESGLGMIVIDYLQLIQGSGREVS EISRSLKALARELEVPVIALSQLSRSVERPMMSDIRESGS IEQDADIVAFLYKNIIEIIIAKQRNGPVGTVQLAFIKEYN KFVNL B:  PPQSIEAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQ KIFHAMLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYL SELADAVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDG YTREDEIDVLLDEADRKIMEITGIPTGFTELDRMTSGFQR SDLIIVAARPSVGKTAFALNIAQNVATKTNENVAIFSLEM SAQQLVMRMLCAEGNINAQNLRTGKLTPEDWGKLTMAMGS LSNAGIYIDDTPSIRVSDIRAKCRRLKQESGLGMIVIDYL QLIQGSGREVSEISRSLKALARELEVPVIALSQLSRSVER PMMSDIRESGSIEQDADIVAFLYKNIIEIIIAKQRNGPVG TVQLAFIKEYNKFVNL C:  PPQSIEAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQ KIFHAMLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYL SELADAVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDG YTREDEIDVLLDEADRKIMEKNIKDILVQTYDNIEMLHNR DGEITGIPTGFTELDRMTSGFQRSDLIIVAARPSVGKTAF ALNIAQNVATKTNENVAIFSLEMSAQQLVMRMLCAEGNIN AQNLRTGKLTPEDWGKLTMAMGSLSNAGIYIDDTPSIRVS DIRAKCRRLKQESGLGMIVIDYLQLIQGSGREVSEISRSL KALARELEVPVIALSQLSRSVERPMMSDIRESGSIEQDAD IVAFLYKNIIEIIIAKQRNGPVGTVQLAFIKEYNKFVNL D:  PPQSIEAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQ KIFHAMLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYL SELADAVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDG YTREDEIDVLLDEADRKIMEITGIPTGFTELDRMTSGFQR SDLIIVAARPSVGKTAFALNIAQNVATKTNENVAIFSLEM SAQQLVMRMLCAEGNINAQNLRTGKLTPEDWGKLTMAMGS LSNAGIYIDDTPSIRVSDIRAKCRRLKQESGLGMIVIDYL QLIQGSGREVSEISRSLKALARELEVPVIALSQLSRSVER PMMSDIRESGSIEQDADIVAFLYKNIIEIIIAKQRNGPVG TVQLAFIKEYNKFVNL E:  PPQSIEAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQ KIFHAMLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYL SELADAVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDG YTREDEIDVLLDEADRKIMEKNIKDILVQTYDNIEEITGI PTGFTELDRMTSGFQRSDLIIVAARPSVGKTAFALNIAQN VATKTNENVAIFSLEMSAQQLVMRMLCAEGNINAQNLRTG KLTPEDWGKLTMAMGSLSNAGIYIDDTPSIRVSDIRAKCR RLKQESGLGMIVIDYLQLIQGSGREVSEISRSLKALAREL EVPVIALSQLSRSVERPMMSDIRESGSIEQDADIVAFLYK NIIEIIIAKQRNGPVGTVQLAFIKEYNKFVNL F:  PPQSIEAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQ KIFHAMLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYL SELADAVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDG YTREDEIDVLLDEADRKIMEKNIKDILVQTYDNIEEITGI PTGFTELDRMTSGFQRSDLIIVAARPSVGKTAFALNIAQN VATKTNENVAIFSLEMSAQQLVMRMLCAEGNINAQNLRTG KLTPEDWGKLTMAMGSLSNAGIYIDDTPSIRVSDIRAKCR RLKQESGLGMIVIDYLQLIQGSGREVSEISRSLKALAREL EVPVIALSQLSRSVERPMMSDIRESGSIEQDADIVAFLYK NIIEIIIAKQRNGPVGTVQLAFIKEYNKFVNL Description Functional site 1) chain A residue 139-147 type prosite sequence LLDEADRKI description DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. LLDEADRkI source prosite : PS00039 2) chain A residue 241 type ACT_SITE sequence E description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 3) chain B residue 241 type ACT_SITE sequence E description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 4) chain C residue 241 type ACT_SITE sequence E description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 5) chain D residue 241 type ACT_SITE sequence E description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 6) chain E residue 241 type ACT_SITE sequence E description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 7) chain F residue 241 type ACT_SITE sequence E description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 9) chain B residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 10) chain B residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 11) chain B residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 12) chain B residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 13) chain B residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 14) chain B residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 15) chain B residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 16) chain B residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 17) chain B residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 18) chain C residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 19) chain A residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 20) chain C residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 21) chain C residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 22) chain C residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 23) chain C residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 24) chain C residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 25) chain C residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 26) chain C residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 27) chain C residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 28) chain D residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 29) chain D residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 30) chain A residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 31) chain D residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 32) chain D residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 33) chain D residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 34) chain D residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 35) chain D residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 36) chain D residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 37) chain D residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 38) chain E residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 39) chain E residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 40) chain E residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 41) chain A residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 42) chain E residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 43) chain E residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 44) chain E residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 45) chain E residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 46) chain E residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 47) chain E residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 48) chain F residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 49) chain F residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 50) chain F residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 51) chain F residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 52) chain A residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 53) chain F residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 54) chain F residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 55) chain F residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 56) chain F residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 57) chain F residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 58) chain A residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 59) chain A residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 60) chain A residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 61) chain A residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 62) chain A residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 63) chain B residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 64) chain C residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 65) chain D residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 66) chain E residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 67) chain F residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 68) chain A residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 69) chain D residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 70) chain D residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 71) chain D residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 72) chain E residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 73) chain E residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 74) chain E residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 75) chain F residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 76) chain F residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 77) chain F residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 78) chain A residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 79) chain A residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 80) chain B residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 81) chain B residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 82) chain B residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 83) chain C residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 84) chain C residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 85) chain C residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 86) chain A residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5 87) chain B residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5 88) chain C residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5 89) chain D residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5 90) chain E residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5 91) chain F residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5

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