eF-site ID 4m4w-ABCDEFGHIJKLMNO PDB Code 4m4w Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O Title Mechanistic implications for the bacterial primosome assembly of the structure of a helicase-helicase loader complex Classification REPLICATION Compound Replicative helicase Source Geobacillus stearothermophilus (Bacillus stearothermophilus) (DNAI_BACSU) Sequence A:  EAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQKIFHA MLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYLSELAD AVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDGYTRED EIDVLLDEADRKIMEITGIPTGFTELDRMTSGFQRSDLII VAARPSVGKTAFALNIAQNVATKTNENVAIFSLEMSAQQL VMRMLCAEGNINAQNLRTGKLTPEDWGKLTMAMGSLSNAG IYIDDTPSIRVSDIRAKCRRLKQESGLGMIVIDYLQLIQE VSEISRSLKALARELEVPVIALSQLRPMMSDIRESGSIEQ DADIVAFLYEIIIAKQRNGPVGTVQLAFIKEYNKFVNL B:  EAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQKIFHA MLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYLSELAD AVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDGYTRED EIDVLLDEADRKIMEITGIPTGFTELDRMTSGFQRSDLII VAARPSVGKTAFALNIAQNVATKTNENVAIFSLEMSAQQL VMRMLCAEGNINAQNLRTGKLTPEDWGKLTMAMGSLSNAG IYIDDTPSIRVSDIRAKCRRLKQESGLGMIVIDYLQLIQE VSEISRSLKALARELEVPVIALSQLRPMMSDIRESGSIEQ DADIVAFLYEIIIAKQRNGPVGTVQLAFIKEYNKFVNL C:  EAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQKIFHA MLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYLSELAD AVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDGYTRED EIDVLLDEADRKIMEITGIPTGFTELDRMTSGFQRSDLII VAARPSVGKTAFALNIAQNVATKTNENVAIFSLEMSAQQL VMRMLCAEGNINAQNLRTGKLTPEDWGKLTMAMGSLSNAG IYIDDTPSIRVSDIRAKCRRLKQESGLGMIVIDYLQLIQE VSEISRSLKALARELEVPVIALSQLRPMMSDIRESGSIEQ DADIVAFLYEIIIAKQRNGPVGTVQLAFIKEYNKFVNL D:  EAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQKIFHA MLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYLSELAD AVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDGYTRED EIDVLLDEADRKIMEITGIPTGFTELDRMTSGFQRSDLII VAARPSVGKTAFALNIAQNVATKTNENVAIFSLEMSAQQL VMRMLCAEGNINAQNLRTGKLTPEDWGKLTMAMGSLSNAG IYIDDTPSIRVSDIRAKCRRLKQESGLGMIVIDYLQLIQE VSEISRSLKALARELEVPVIALSQLRPMMSDIRESGSIEQ DADIVAFLYEIIIAKQRNGPVGTVQLAFIKEYNKFVNL E:  EAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQKIFHA MLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYLSELAD AVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDGYTRED EIDVLLDEADRKIMEITGIPTGFTELDRMTSGFQRSDLII VAARPSVGKTAFALNIAQNVATKTNENVAIFSLEMSAQQL VMRMLCAEGNINAQNLRTGKLTPEDWGKLTMAMGSLSNAG IYIDDTPSIRVSDIRAKCRRLKQESGLGMIVIDYLQLIQE VSEISRSLKALARELEVPVIALSQLRPMMSDIRESGSIEQ DADIVAFLYEIIIAKQRNGPVGTVQLAFIKEYNKFVNL F:  EAEQAVLGAVFLDPAALVPASEILIPEDFYRAAHQKIFHA MLRVADRGEPVDLVTVTAELAASEQLEEIGGVSYLSELAD AVPTAANVEYYARIVEEKSVLRRLIRTATSIAQDGYTRED EIDVLLDEADRKIMEITGIPTGFTELDRMTSGFQRSDLII VAARPSVGKTAFALNIAQNVATKTNENVAIFSLEMSAQQL VMRMLCAEGNINAQNLRTGKLTPEDWGKLTMAMGSLSNAG IYIDDTPSIRVSDIRAKCRRLKQESGLGMIVIDYLQLIQE VSEISRSLKALARELEVPVIALSQLRPMMSDIRESGSIEQ DADIVAFLYEIIIAKQRNGPVGTVQLAFIKEYNKFVNL G:  LLPAFQNAERLLLAHXXRSRDVALVVQERIGGRFNIEEHR ALAAYIYAFYEEGHEADPGALISRIPGELQPLASELSLLL IADDVSEQELEDYIRHVLNRPKWLXLKVKEQEKTEAERRK DFLTAARIAKEXIEXKKX H:  LLPAFQNAERLLLAHXXRSRDVALVVQERIGGRFNIEEHR ALAAYIYAFYEEGHEADPGALISRIPGELQPLASELSLLL IADDVSEQELEDYIRHVLNRPKWLXLKVKEQEKTEAERRK DFLTAARIAKEXIEXKKX I:  LLPAFQNAERLLLAHXXRSRDVALVVQERIGGRFNIEEHR ALAAYIYAFYEEGHEADPGALISRIPGELQPLASELSLLL IADDVSEQELEDYIRHVLNRPKWLXLKVKEQEKTEAERRK DFLTAARIAKEXIEXKKX J:  QDVQAFLKENEEVIDQKMIEKSLNKLYEYIEQSKNCSGYH PKLVVNGRSIDIEYYECKKQQSLMKSMYIQQDLLGATFQQ VDISDPSRLAMFQHVTDFLKSYNETGKGKGLYLYGKFGVG KTFMLAAIANELAEKEYSSMIVYVPEFVRELKNSQTLEEK LNMVKTTPVLMLDDIGAESWVRDEVIGTVLQHRMSQQLPT FFSSNFSPDELKHHFTYSQEVKAARLMERILYLAAPIRLD GENRR K:  QDVQAFLKENEEVIDQKMIEKSLNKLYEYIEQSKNCSGYH PKLVVNGRSIDIEYYECPVKKQQSLMKSMYIQQDLLGATF QQVDISDPSRLAMFQHVTDFLKSYNETGKGKGLYLYGKFG VGKTFMLAAIANELAEKEYSSMIVYVPEFVRELKNSLQDQ TLEEKLNMVKTTPVLMLDDIGAESTSWVRDEVIGTVLQHR MSQQLPTFFSSNFSPDELKHHFTYEKEEVKAARLMERILY LAAPIRLD L:  QDVQAFLKENEEVIDQKMIEKSLNKLYEYIEQSKNCSYCG YHPKLVVNGRSIDIEYYECKKQQSLMKSMYIQQDLLGATF QQVDISDPSRLAMFQHVTDFLKSYNETGKGKGLYLYGKFG VGKTFMLAAIANELAEKEYSSMIVYVPEFVRELKNSQTLE EKLNMVKTTPVLMLDDIGAESWVRDEVIGTVLQHRMSQQL PTFFSSNFSPDELKHHFTYSQEVKAARLMERILYLAAPIR LDGENRR M:  QDVQAFLKENEEVIDQKMIEKSLNKLYEYIEQSKNCSYCG YHPKLVVNGRSIDIEYYECKQQSLMKSMYIQQDLLGATFQ QVDISDPSRLAMFQHVTDFLKSYNETGKGKGLYLYGKFGV GKTFMLAAIANELAEKEYSSMIVYVPEFVRELKNSLQDQT LEEKLNMVKTTPVLMLDDIGAESTSWVRDEVIGTVLQHRM SQQLPTFFSSNFSPDELKHHFTYEKEEVKAARLMERILYL AAPIRLD N:  QDVQAFLKENEEVIDQKMIEKSLNKLYEYIEQSKNCSYCG YHPKLVVNGRSIDIEYKKQQSLMKSMYIQQDLLGATFQQV DISDPSRLAMFQHVTDFLKSYNETGKGKGLYLYGKFGVGK TFMLAAIANELAEKEYSSMIVYVPEFVRELKNSQTLEEKL NMVKTTPVLMLDDIGAESWVRDEVIGTVLQHRMSQQLPTF FSSNFSPDELKHHFTYSQEVKAARLMERILYLAAPIRLDG ENRR O:  QDVQAFLKENEEVIDQKMIEKSLNKLYEYIEQSKNCSYCG YHPKLVVNGRSIDIEYYECPVKKQQSLMKSMYIQQDLLGA TFQQVDISDPSRLAMFQHVTDFLKSYNETGKGKGLYLYGK FGVGKTFMLAAIANELAEKEYSSMIVYVPEFVRELKNSLQ DQTLEEKLNMVKTTPVLMLDDIGAESTSWVRDEVIGTVLQ HRMSQQLPTFFSSNFSPDELKHHFTYEKEEVKAARLMERI LYLAAPIRLD Description (1)  Replicative helicase, DNA primase (E.C.2.7.7.-), Primosomal protein DnaI 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 L residue 70 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 4) chain L residue 84 type ACT_SITE sequence H description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 5) chain L residue 101 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 6) chain M residue 67 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 7) chain M residue 70 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 8) chain M residue 84 type ACT_SITE sequence H description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 9) chain M residue 101 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 10) chain N residue 67 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 11) chain N residue 70 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 12) chain N residue 84 type ACT_SITE sequence H description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 13) 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 14) chain O residue 67 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 15) chain O residue 70 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 16) chain O residue 84 type ACT_SITE sequence H description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 17) chain O residue 101 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 18) 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 19) 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 20) 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 21) 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 22) chain K residue 84 type ACT_SITE sequence H description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 23) chain K residue 101 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 24) chain L residue 67 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 26) chain B residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 27) chain B residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 28) chain B residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 29) chain B residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 30) chain B residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 31) chain B residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 32) chain B residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 33) chain B residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 34) chain B residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 35) chain C residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 36) chain A residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 37) chain C residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 38) chain C residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 39) chain C residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 40) chain C residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 41) chain C residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 42) chain C residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 43) chain C residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 44) chain C residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 45) chain D residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 46) chain D residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 47) chain A residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 48) chain D residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 49) chain D residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 50) chain D residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 51) chain D residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 52) chain D residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 53) chain D residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 54) chain D residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 55) chain E residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 56) chain E residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 57) chain E residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 58) chain A residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 59) chain E residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 60) chain E residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 61) chain E residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 62) chain E residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 63) chain E residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 64) chain E residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 65) chain F residue 213 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 66) chain F residue 215 type BINDING sequence G description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 67) chain F residue 216 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 68) chain F residue 217 type BINDING sequence T description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 69) chain A residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 70) chain F residue 218 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 71) chain F residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 72) chain F residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 73) chain F residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 74) chain F residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 75) chain A residue 250 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 76) chain A residue 418 type BINDING sequence K description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 77) chain A residue 419 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 78) chain A residue 420 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI2 79) chain A residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 80) chain B residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 81) chain C residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 82) chain D residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 83) chain E residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 84) chain F residue 362 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:23022319 source Swiss-Prot : SWS_FT_FI3 85) chain A residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 86) chain D residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 87) chain D residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 88) chain D residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 89) chain E residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 90) chain E residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 91) chain E residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 92) chain F residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 93) chain F residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 94) chain F residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 95) chain A residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 96) chain A residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 97) chain B residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 98) chain B residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 99) chain B residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 100) chain C residue 381 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 101) chain C residue 382 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 102) chain C residue 384 type BINDING sequence G description BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV source Swiss-Prot : SWS_FT_FI4 103) chain A residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5 104) chain B residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5 105) chain C residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5 106) chain D residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5 107) chain E residue 362 type SITE sequence Q description Gamma-phosphate sensor => ECO:0000305|PubMed:12235389 source Swiss-Prot : SWS_FT_FI5 108) 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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