eF-site ID 2f48-B
PDB Code 2f48
Chain B

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Title Crystal Structure of A Novel Fructose 1,6-Bisphosphate and AlF3 containing Pyrophosphate-dependent Phosphofructo-1-kinase Complex from Borrelia burgdorferi
Classification TRANSFERASE
Compound diphosphate--fructose-6-phosphate 1-phosphotransferase
Source Borrelia burgdorferi (Lyme disease spirochete) (O51052_BORBU)
Sequence B:  TSLFKQERQKYIPKLPNILKKDFNNISLVYGENTEAIQDR
QALKEFFKNTYGLPIISFTEGESSLSFSKALNIGIILSGG
PAPGGHNVISGVFDAIKKFNPNSKLFGFKGGPLGLLENDK
IELTESLINSYRNTGGFDIVSSGRTKIETEEHYNKALFVA
KENNLNAIIIIGGDDSNTNAAILAEYFKKNGENIQVIGVP
KTIDADLRNDHIEISFGFDSATKIYSELIGNLCRDAMSTK
KYWHFVKLMGRSASHVALECALKTHPNICIVSEEVLAKKK
TLSEIIDEMVSVILKRSLNGDNFGVVIVPEGLIEFIPEVK
SLMLELCDIFDKNEGEFKGLNIEKMKEIFVAKLSDYMKGV
YLSLPLFIQFELIKSILERDPHGNFNVSRVPTEKLFIEMI
QSRLNDMKKRGEYKGSFTPVDHFFGYEGRSAFPSNFDSDY
CYSLGYNAVVLILNGLTGYMSCIKNLNLKPTDWIAGGVPL
TMLMNMEERYGEKKPVIKKALVDLEGRPFKEFVKNRDKWA
LNNLYLYPGPVQYFGSSEIVDEITETLKLELF
Description


Functional site

1) chain B
residue 82
type catalytic
sequence G
description 653
source MCSA : MCSA2

2) chain B
residue 146
type catalytic
sequence R
description 653
source MCSA : MCSA2

3) chain B
residue 177
type catalytic
sequence D
description 653
source MCSA : MCSA2

4) chain B
residue 203
type catalytic
sequence K
description 653
source MCSA : MCSA2

5) chain B
residue 204
type catalytic
sequence T
description 653
source MCSA : MCSA2

6) chain B
residue 206
type catalytic
sequence D
description 653
source MCSA : MCSA2

7) chain B
residue 206
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-Rule:MF_01980
source Swiss-Prot : SWS_FT_FI1

8) chain B
residue 82
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
source Swiss-Prot : SWS_FT_FI2

9) chain B
residue 243
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
source Swiss-Prot : SWS_FT_FI2

10) chain B
residue 146
type BINDING
sequence R
description in other chain => ECO:0000269|Ref.5
source Swiss-Prot : SWS_FT_FI3

11) chain B
residue 176
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-Rule:MF_01980
source Swiss-Prot : SWS_FT_FI4

12) chain B
residue 204
type BINDING
sequence T
description in other chain => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
source Swiss-Prot : SWS_FT_FI5

13) chain B
residue 251
type BINDING
sequence M
description in other chain => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
source Swiss-Prot : SWS_FT_FI5

14) chain B
residue 312
type BINDING
sequence E
description in other chain => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
source Swiss-Prot : SWS_FT_FI5

15) chain B
residue 428
type BINDING
sequence Y
description in other chain => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
source Swiss-Prot : SWS_FT_FI5

16) chain B
residue 177
type SITE
sequence D
description Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000305|PubMed:12015149
source Swiss-Prot : SWS_FT_FI6

17) chain B
residue 203
type SITE
sequence K
description Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000305|PubMed:12015149
source Swiss-Prot : SWS_FT_FI7


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