eF-site ID 4esv-A PDB Code 4esv Chain A click to enlarge Title A New Twist on the Translocation Mechanism of Helicases from the Structure of DnaB with its Substrates Classification HYDROLASE/DNA Compound 5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3' Source (4ESV) Sequence A:  SERIPPQSIEAEQAVLGAVFLDPAALVPASEILIPEDFYR AAHQKIFHAMLRVADRGEPVDLVTVTAELAASEQLEEIGG VSYLSELADAVPTAANVEYYARIVEEKSVLRRLIRTATSI AQDGYTREDEIDVLLDEADRKIMEVSQFKNIKDILVQTYI TGIPTGFTELDRMTSGFQRSDLIIVAARPSVGKTAFALNI AQNVATKTNENVAIFSLEMSAQQLVMRMLCAEGNINAQNL RTGKLTPEDWGKLTMAMGSLSNAGIYIDDTPSIRVSDIRA KCRRLKQESGLGMIVIDYLQLIQGSGRSKENRQQEVSEIS RSLKALARELEVPVIALSQLSRSVEQRQDKRPMMSDIRES GSIEQDADIVAFLYRDDYYNKDSENKNIIEIIIAKQRNGP VGTVQLAFIKEYNKFVNL Description Functional site 1) chain A residue 213 type sequence S description BINDING SITE FOR RESIDUE GDP A 502 source : AC2 2) chain A residue 214 type sequence V description BINDING SITE FOR RESIDUE GDP A 502 source : AC2 3) chain A residue 215 type sequence G description BINDING SITE FOR RESIDUE GDP A 502 source : AC2 4) chain A residue 216 type sequence K description BINDING SITE FOR RESIDUE GDP A 502 source : AC2 5) chain A residue 217 type sequence T description BINDING SITE FOR RESIDUE GDP A 502 source : AC2 6) chain A residue 218 type sequence A description BINDING SITE FOR RESIDUE GDP A 502 source : AC2 7) chain A residue 250 type sequence R description BINDING SITE FOR RESIDUE GDP A 502 source : AC2 8) chain A residue 260 type sequence A description BINDING SITE FOR RESIDUE GDP A 502 source : AC2 9) chain A residue 261 type sequence Q description BINDING SITE FOR RESIDUE GDP A 502 source : AC2 10) chain A residue 431 type sequence F description BINDING SITE FOR RESIDUE GDP A 502 source : AC2 11) chain A residue 433 type sequence K description BINDING SITE FOR RESIDUE GDP A 502 source : AC2 12) chain A residue 217 type sequence T description BINDING SITE FOR RESIDUE CA A 503 source : AC3 13) chain A residue 241 type sequence E description BINDING SITE FOR RESIDUE CA A 503 source : AC3 14) chain A residue 320 type sequence D description BINDING SITE FOR RESIDUE CA A 503 source : AC3 15) chain A residue 212 type sequence P description BINDING SITE FOR RESIDUE ALF A 504 source : AC4 16) chain A residue 213 type sequence S description BINDING SITE FOR RESIDUE ALF A 504 source : AC4 17) chain A residue 216 type sequence K description BINDING SITE FOR RESIDUE ALF A 504 source : AC4 18) chain A residue 241 type sequence E description BINDING SITE FOR RESIDUE ALF A 504 source : AC4 19) chain A residue 362 type sequence Q description BINDING SITE FOR RESIDUE ALF A 504 source : AC4 20) chain A residue 378 type sequence S description BINDING SITE FOR RESIDUE CA A 505 source : AC5 21) chain A residue 213 type sequence S description BINDING SITE FOR RESIDUE CA A 506 source : AC6 22) chain A residue 111 type sequence E description BINDING SITE FOR RESIDUE CA A 507 source : AC7 23) chain A residue 391 type sequence D description BINDING SITE FOR RESIDUE CA A 507 source : AC7 24) chain A residue 139-147 type prosite sequence LLDEADRKI description DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. LLDEADRkI source prosite : PS00039 25) 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 26) chain A residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 27) chain A residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 28) chain A residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 29) chain A residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 30) chain A residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 31) chain A residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 32) chain A residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 33) chain A residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 34) chain A residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 35) chain A residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 37) chain A residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 38) chain A residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 39) chain A residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5

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