eF-site ID 1alj-A PDB Code 1alj Chain A click to enlarge Title ALKALINE PHOSPHATASE MUTANT (H412N) Classification HYDROLASE (PHOSPHORIC MONOESTER) Compound ALKALINE PHOSPHATASE Source Escherichia coli (strain K12) (PPB_ECOLI) Sequence A:  MPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAK NIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQ YTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVD IHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHV TSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVT LGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASL NSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPA VTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEG ASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEGNTL VIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYG NSEEDSQENTGSQLRIAAYGPHAANVVGLTDQTDLFYTMK AALGLK Description Functional site 1) chain A residue 327 type sequence D description CATALYTICALLY ACTIVE SITE ON A SUBUNIT source : A 2) chain A residue 331 type sequence H description CATALYTICALLY ACTIVE SITE ON A SUBUNIT source : A 3) chain A residue 412 type sequence N description CATALYTICALLY ACTIVE SITE ON A SUBUNIT source : A 4) chain A residue 51 type sequence D description CATALYTICALLY ACTIVE SITE ON A SUBUNIT source : A 5) chain A residue 369 type sequence D description CATALYTICALLY ACTIVE SITE ON A SUBUNIT source : A 6) chain A residue 370 type sequence H description CATALYTICALLY ACTIVE SITE ON A SUBUNIT source : A 7) chain A residue 155 type sequence T description CATALYTICALLY ACTIVE SITE ON A SUBUNIT source : A 8) chain A residue 322 type sequence E description CATALYTICALLY ACTIVE SITE ON A SUBUNIT source : A 9) chain A residue 166 type sequence R description CATALYTICALLY ACTIVE SITE ON A SUBUNIT source : A 10) chain A residue 102 type sequence S description CATALYTICALLY ACTIVE SITE ON A SUBUNIT source : A 11) chain A residue 51 type sequence D description BINDING SITE FOR RESIDUE ZN A 451 source : AC1 12) chain A residue 102 type sequence S description BINDING SITE FOR RESIDUE ZN A 451 source : AC1 13) chain A residue 327 type sequence D description BINDING SITE FOR RESIDUE ZN A 451 source : AC1 14) chain A residue 369 type sequence D description BINDING SITE FOR RESIDUE ZN A 451 source : AC1 15) chain A residue 370 type sequence H description BINDING SITE FOR RESIDUE ZN A 451 source : AC1 16) chain A residue 51 type sequence D description BINDING SITE FOR RESIDUE MG A 452 source : AC2 17) chain A residue 153 type sequence D description BINDING SITE FOR RESIDUE MG A 452 source : AC2 18) chain A residue 155 type sequence T description BINDING SITE FOR RESIDUE MG A 452 source : AC2 19) chain A residue 322 type sequence E description BINDING SITE FOR RESIDUE MG A 452 source : AC2 20) chain A residue 101 type sequence D description BINDING SITE FOR RESIDUE PO4 A 453 source : AC3 21) chain A residue 102 type sequence S description BINDING SITE FOR RESIDUE PO4 A 453 source : AC3 22) chain A residue 166 type sequence R description BINDING SITE FOR RESIDUE PO4 A 453 source : AC3 23) chain A residue 327 type sequence D description BINDING SITE FOR RESIDUE PO4 A 453 source : AC3 24) chain A residue 331 type sequence H description BINDING SITE FOR RESIDUE PO4 A 453 source : AC3 25) chain A residue 370 type sequence H description BINDING SITE FOR RESIDUE PO4 A 453 source : AC3 26) chain A residue 412 type sequence N description BINDING SITE FOR RESIDUE PO4 A 453 source : AC3 27) chain A residue 51 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 28) chain A residue 153 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 29) chain A residue 155 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 30) chain A residue 322 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 31) chain A residue 327 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 32) chain A residue 331 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 33) chain A residue 369 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 34) chain A residue 370 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 35) chain A residue 412 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 36) chain A residue 102 type ACT_SITE sequence S description Phosphoserine intermediate source Swiss-Prot : SWS_FT_FI1 37) chain A residue 51 type catalytic sequence D description 44 source MCSA : MCSA1 38) chain A residue 369 type catalytic sequence D description 44 source MCSA : MCSA1 39) chain A residue 370 type catalytic sequence H description 44 source MCSA : MCSA1 40) chain A residue 412 type catalytic sequence N description 44 source MCSA : MCSA1 41) chain A residue 102 type catalytic sequence S description 44 source MCSA : MCSA1 42) chain A residue 153 type catalytic sequence D description 44 source MCSA : MCSA1 43) chain A residue 155 type catalytic sequence T description 44 source MCSA : MCSA1 44) chain A residue 166 type catalytic sequence R description 44 source MCSA : MCSA1 45) chain A residue 322 type catalytic sequence E description 44 source MCSA : MCSA1 46) chain A residue 327 type catalytic sequence D description 44 source MCSA : MCSA1 47) chain A residue 328 type catalytic sequence K description 44 source MCSA : MCSA1 48) chain A residue 331 type catalytic sequence H description 44 source MCSA : MCSA1 49) chain A residue 99-107 type prosite sequence VTDSAASAT description ALKALINE_PHOSPHATASE Alkaline phosphatase active site. VtDSAASAT source prosite : PS00123

Display surface Download Links