eF-site ID 2f48-B PDB Code 2f48 Chain B click to enlarge 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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