eF-site ID 2r6d-ABCDEF
PDB Code 2r6d
Chain A, B, C, D, E, F

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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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