eF-site ID 1ajd-B PDB Code 1ajd Chain B click to enlarge Title THREE-DIMENSIONAL STRUCTURE OF THE D153G MUTANT OF E. COLI ALKALINE PHOSPHATASE: A MUTANT WITH WEAKER MAGNESIUM BINDING AND INCREASED CATALYTIC ACTIVITY Classification NON SPECIFIC MONO-ESTERASE Compound ALKALINE PHOSPHATASE INTERMEDIATE II OF HOLO ENZYME Source Escherichia coli (strain K12) (PPB_ECOLI) Sequence B:  TPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDK PAKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPL TGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGAL GVDIHEKDHPTILEMAKAAGLATGNVSTAELQGATPAALV AHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARA DVTLGGGAKTFAETATAGEWQGKTLREQAEARGYQLVSDA ASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNID KPAVTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQ VEGASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEG NTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVM SYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFY TMKAALGLK Description Functional site 1) chain B residue 327 type sequence D description BINDING SITE FOR RESIDUE ZN B 950 source : AC4 2) chain B residue 331 type sequence H description BINDING SITE FOR RESIDUE ZN B 950 source : AC4 3) chain B residue 412 type sequence H description BINDING SITE FOR RESIDUE ZN B 950 source : AC4 4) chain B residue 51 type sequence D description BINDING SITE FOR RESIDUE ZN B 951 source : AC5 5) chain B residue 102 type sequence S description BINDING SITE FOR RESIDUE ZN B 951 source : AC5 6) chain B residue 327 type sequence D description BINDING SITE FOR RESIDUE ZN B 951 source : AC5 7) chain B residue 369 type sequence D description BINDING SITE FOR RESIDUE ZN B 951 source : AC5 8) chain B residue 370 type sequence H description BINDING SITE FOR RESIDUE ZN B 951 source : AC5 9) chain B residue 51 type sequence D description BINDING SITE FOR RESIDUE MG B 952 source : AC6 10) chain B residue 155 type sequence T description BINDING SITE FOR RESIDUE MG B 952 source : AC6 11) chain B residue 322 type sequence E description BINDING SITE FOR RESIDUE MG B 952 source : AC6 12) chain B residue 51 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 13) chain B residue 153 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 14) chain B residue 155 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 15) chain B residue 322 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 16) chain B residue 327 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 17) chain B residue 331 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 18) chain B residue 369 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 19) chain B residue 370 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 20) chain B residue 412 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 21) chain B residue 102 type ACT_SITE sequence S description Phosphoserine intermediate source Swiss-Prot : SWS_FT_FI1 22) chain B residue 51 type catalytic sequence D description 44 source MCSA : MCSA2 23) chain B residue 369 type catalytic sequence D description 44 source MCSA : MCSA2 24) chain B residue 370 type catalytic sequence H description 44 source MCSA : MCSA2 25) chain B residue 412 type catalytic sequence H description 44 source MCSA : MCSA2 26) chain B residue 102 type catalytic sequence S description 44 source MCSA : MCSA2 27) chain B residue 153 type catalytic sequence G description 44 source MCSA : MCSA2 28) chain B residue 155 type catalytic sequence T description 44 source MCSA : MCSA2 29) chain B residue 166 type catalytic sequence R description 44 source MCSA : MCSA2 30) chain B residue 322 type catalytic sequence E description 44 source MCSA : MCSA2 31) chain B residue 327 type catalytic sequence D description 44 source MCSA : MCSA2 32) chain B residue 328 type catalytic sequence K description 44 source MCSA : MCSA2 33) chain B residue 331 type catalytic sequence H description 44 source MCSA : MCSA2

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