eF-site ID 2l5h_2-AB
PDB Code 2l5h
Model 2
Chain A, B

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Title Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering
Classification TRANSFERASE
Compound Phosphoenolpyruvate-protein phosphotransferase
Source Escherichia coli (strain K12) (PT1_ECOLI)
Sequence A:  MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEV
ERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLL
EDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD
EYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVA
ADLTPSETAQLNLKKVLGFITDAGGRTSQTSIMARSLELP
AIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR
AVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRD
VEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAV
AEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAI
RIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVR
ALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIAR
HLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPS
VLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGL
DEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDE
LMTLVNKFIEEKT
B:  MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEV
ERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLL
EDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD
EYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVA
ADLTPSETAQLNLKKVLGFITDAGGRTSQTSIMARSLELP
AIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR
AVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRD
VEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAV
AEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAI
RIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVR
ALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIAR
HLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPS
VLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGL
DEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDE
LMTLVNKFIEEKT
Description


Functional site

1) chain A
residue 189
type catalytic
sequence Q
description 920
source MCSA : MCSA1

2) chain A
residue 431
type catalytic
sequence E
description 920
source MCSA : MCSA1

3) chain A
residue 455
type catalytic
sequence D
description 920
source MCSA : MCSA1

4) chain A
residue 502
type catalytic
sequence C
description 920
source MCSA : MCSA1

5) chain B
residue 189
type catalytic
sequence Q
description 920
source MCSA : MCSA2

6) chain B
residue 431
type catalytic
sequence E
description 920
source MCSA : MCSA2

7) chain B
residue 455
type catalytic
sequence D
description 920
source MCSA : MCSA2

8) chain B
residue 502
type catalytic
sequence C
description 920
source MCSA : MCSA2

9) chain A
residue 447-465
type prosite
sequence DFFSIGTNDLTQYTLAVDR
description PEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSIGTNDLtQYTLAvdR
source prosite : PS00742

10) chain A
residue 189
type ACT_SITE
sequence Q
description Tele-phosphohistidine intermediate => ECO:0000269|PubMed:12705838, ECO:0000269|PubMed:17053069
source Swiss-Prot : SWS_FT_FI1

11) chain B
residue 189
type ACT_SITE
sequence Q
description Tele-phosphohistidine intermediate => ECO:0000269|PubMed:12705838, ECO:0000269|PubMed:17053069
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 502
type ACT_SITE
sequence C
description Proton donor => ECO:0000269|PubMed:12705838, ECO:0000305|PubMed:17053069
source Swiss-Prot : SWS_FT_FI2

13) chain B
residue 502
type ACT_SITE
sequence C
description Proton donor => ECO:0000269|PubMed:12705838, ECO:0000305|PubMed:17053069
source Swiss-Prot : SWS_FT_FI2

14) chain A
residue 296
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P23533
source Swiss-Prot : SWS_FT_FI3

15) chain A
residue 465
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P23533
source Swiss-Prot : SWS_FT_FI3

16) chain B
residue 296
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P23533
source Swiss-Prot : SWS_FT_FI3

17) chain B
residue 465
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P23533
source Swiss-Prot : SWS_FT_FI3

18) chain A
residue 332
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17053069
source Swiss-Prot : SWS_FT_FI4

19) chain A
residue 431
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17053069
source Swiss-Prot : SWS_FT_FI4

20) chain A
residue 454
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:17053069
source Swiss-Prot : SWS_FT_FI4

21) chain A
residue 455
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:17053069
source Swiss-Prot : SWS_FT_FI4

22) chain B
residue 332
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17053069
source Swiss-Prot : SWS_FT_FI4

23) chain B
residue 431
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17053069
source Swiss-Prot : SWS_FT_FI4

24) chain B
residue 454
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:17053069
source Swiss-Prot : SWS_FT_FI4

25) chain B
residue 455
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:17053069
source Swiss-Prot : SWS_FT_FI4


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