eF-site ID 2r6d-A PDB Code 2r6d Chain A 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 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 A residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 4) chain A residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 5) chain A residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 6) chain A residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 7) chain A residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 8) chain A residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 9) chain A residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 10) chain A residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 11) chain A residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 12) chain A residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 14) chain A residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 15) chain A residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 16) 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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