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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