eF-site ID 1qas-AB PDB Code 1qas Chain A, B click to enlarge Title 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1 Classification HYDROLASE Compound PHOSPHOLIPASE C DELTA-1 Source null (PLCD1_RAT) Sequence A:  YKMLTQRAEIDRAFEEAAGSAETLSVERLVTFLQHQQREE EAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADG NAFSLAHRRVYQDMDQPLSHYLVSSSHNTYLLEDQLTGPS STEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKI LFCDVLRAIRDYAFKASPYPVILSLENHCSLEQQRVMARH LRAILGPILLDQPLDGVTTSLPSPEQLKGKILLKGKKLGG KLVPELSDMIIYCKSVHFGGFSSPGTSGQAFYEMASFSES RALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVE MWNGGCQIVALNFQTPGPEMDVYLGCFQDNGGCGYVLKPA FLRDPNTTFNSRALTQGPWWRPERLRVRIISGQQLPKVNI VDPKVIVEIHGVGRDTGSRQTAVITNNGFNPRWDMEFEFE VTVPDLALVRFMVEDYDSSSKNDFIGQSTIPWNSLKQGYR HVHLLSKNGDQHPSATLFVKISIQD B:  KMLTQRAEIDRAFEEAAGSAETLSVERLVTFLQHQQREEE AGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGN AFSLAHRRVYQDMDQPLSHYLVSSSHNTYLLEDQLTGPSS TEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKIL FCDVLRAIRDYAFKASPYPVILSLENHCSLEQQRVMARHL RAILGPILLDQPLDGVTTSLPSPEQLKGKILLKGKKLGGL KLKLVPELSDMIIYCKSVHFGGFSSPGQAFYEMASFSESR ALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEM WNGGCQIVALNFQTPGPEMDVYLGCFQDNGGCGYVLKPAF LRDPNTTFNSRALTQGPWWRPERLRVRIISGQQLPKVNIV DPKVIVEIHGVGRDTGSRQTAVITNNGFNPRWDMEFEFEV TVPDLALVRFMVEDYDSSSKNDFIGQSTIPWNSLKQGYRH VHLLSKNGDQHPSATLFVKISIQD Description Functional site 1) chain A residue 311 type catalytic sequence H description 28 source MCSA : MCSA1 2) chain A residue 312 type catalytic sequence N description 28 source MCSA : MCSA1 3) chain A residue 341 type catalytic sequence E description 28 source MCSA : MCSA1 4) chain A residue 343 type catalytic sequence D description 28 source MCSA : MCSA1 5) chain A residue 356 type catalytic sequence H description 28 source MCSA : MCSA1 6) chain A residue 390 type catalytic sequence E description 28 source MCSA : MCSA1 7) chain B residue 311 type catalytic sequence H description 28 source MCSA : MCSA2 8) chain B residue 312 type catalytic sequence N description 28 source MCSA : MCSA2 9) chain B residue 341 type catalytic sequence E description 28 source MCSA : MCSA2 10) chain B residue 343 type catalytic sequence D description 28 source MCSA : MCSA2 11) chain B residue 356 type catalytic sequence H description 28 source MCSA : MCSA2 12) chain B residue 390 type catalytic sequence E description 28 source MCSA : MCSA2 13) chain B residue 311 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI1 14) chain B residue 356 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI1 15) chain A residue 311 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI1 16) chain A residue 356 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI1 17) chain A residue 653 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 18) chain A residue 438 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 19) chain A residue 440 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 20) chain A residue 522 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 21) chain A residue 549 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 22) chain A residue 651 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI3 23) chain A residue 343 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 24) chain A residue 390 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 25) chain A residue 677 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 26) chain A residue 706 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 27) chain A residue 707 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 28) chain A residue 708 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 29) chain B residue 312 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 30) chain B residue 341 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 31) chain B residue 343 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 32) chain B residue 390 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 33) chain B residue 438 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 34) chain B residue 440 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 35) chain B residue 522 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 36) chain B residue 549 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 37) chain B residue 651 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI3 38) chain B residue 653 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 39) chain B residue 677 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 40) chain B residue 706 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 41) chain B residue 707 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 42) chain B residue 708 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 43) chain A residue 312 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 44) chain A residue 341 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3

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