eF-site ID 1swv-AB PDB Code 1swv Chain A, B click to enlarge Title Crystal structure of the D12A mutant of phosphonoacetaldehyde hydrolase complexed with magnesium Classification HYDROLASE Compound phosphonoacetaldehyde hydrolase Source Bacillus cereus (O31156_BACCE) Sequence A:  KIEAVIFAWAGTTVDYGCFAPLEVFMEIFHKRGVAITAEE ARKPMGLLKIDHVRALTEMPRIASEWNRVFRQLPTEADIQ EMYEEFEEILFAILPRYASPINGVKEVIASLRERGIKIGS TTGYTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYPW MCYKNAMELGVYPMNHMIKVGDTVSDMKEGRNAGMWTVGV ILGSSELGLTEEEVENMDSVELREKIEVVRNRFVENGAHF TIETMQELESVMEHIEK B:  KIEAVIFAWAGTTVDYGCFAPLEVFMEIFHKRGVAITAEE ARKPMGLLKIDHVRALTEMPRIASEWNRVFRQLPTEADIQ EMYEEFEEILFAILPRYASPINGVKEVIASLRERGIKIGS TTGYTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYPW MCYKNAMELGVYPMNHMIKVGDTVSDMKEGRNAGMWTVGV ILGSSELGLTEEEVENMDSVELREKIEVVRNRFVENGAHF TIETMQELESVMEHIEK Description Functional site 1) chain A residue 12 type sequence A description BINDING SITE FOR RESIDUE MG A 501 source : AC1 2) chain A residue 14 type sequence A description BINDING SITE FOR RESIDUE MG A 501 source : AC1 3) chain A residue 186 type sequence D description BINDING SITE FOR RESIDUE MG A 501 source : AC1 4) chain A residue 190 type sequence D description BINDING SITE FOR RESIDUE MG A 501 source : AC1 5) chain B residue 12 type sequence A description BINDING SITE FOR RESIDUE MG B 502 source : AC2 6) chain B residue 14 type sequence A description BINDING SITE FOR RESIDUE MG B 502 source : AC2 7) chain B residue 186 type sequence D description BINDING SITE FOR RESIDUE MG B 502 source : AC2 8) chain B residue 187 type sequence T description BINDING SITE FOR RESIDUE MG B 502 source : AC2 9) chain B residue 190 type sequence D description BINDING SITE FOR RESIDUE MG B 502 source : AC2 10) chain A residue 12 type catalytic sequence A description 181 source MCSA : MCSA1 11) chain A residue 14 type catalytic sequence A description 181 source MCSA : MCSA1 12) chain A residue 45 type catalytic sequence A description 181 source MCSA : MCSA1 13) chain A residue 49 type catalytic sequence M description 181 source MCSA : MCSA1 14) chain A residue 53 type catalytic sequence K description 181 source MCSA : MCSA1 15) chain A residue 56 type catalytic sequence H description 181 source MCSA : MCSA1 16) chain A residue 160 type catalytic sequence R description 181 source MCSA : MCSA1 17) chain A residue 186 type catalytic sequence D description 181 source MCSA : MCSA1 18) chain B residue 12 type catalytic sequence A description 181 source MCSA : MCSA2 19) chain B residue 14 type catalytic sequence A description 181 source MCSA : MCSA2 20) chain B residue 45 type catalytic sequence A description 181 source MCSA : MCSA2 21) chain B residue 49 type catalytic sequence M description 181 source MCSA : MCSA2 22) chain B residue 53 type catalytic sequence K description 181 source MCSA : MCSA2 23) chain B residue 56 type catalytic sequence H description 181 source MCSA : MCSA2 24) chain B residue 160 type catalytic sequence R description 181 source MCSA : MCSA2 25) chain B residue 186 type catalytic sequence D description 181 source MCSA : MCSA2 26) chain A residue 12 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI3 27) chain A residue 14 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI3 28) chain A residue 186 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 29) chain B residue 12 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI3 30) chain B residue 14 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI3 31) chain B residue 186 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 32) chain A residue 12 type ACT_SITE sequence A description Nucleophile source Swiss-Prot : SWS_FT_FI1 33) chain B residue 12 type ACT_SITE sequence A description Nucleophile source Swiss-Prot : SWS_FT_FI1 34) chain A residue 53 type ACT_SITE sequence K description Schiff-base intermediate with substrate source Swiss-Prot : SWS_FT_FI2 35) chain B residue 53 type ACT_SITE sequence K description Schiff-base intermediate with substrate source Swiss-Prot : SWS_FT_FI2

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