eF-site ID 1kfq-AB PDB Code 1kfq Chain A, B click to enlarge Title Crystal Structure of Exocytosis-Sensitive Phosphoprotein, pp63/parafusin (Phosphoglucomutse) from Paramecium. OPEN FORM Classification ISOMERASE Compound phosphoglucomutase 1 Source Paramecium tetraurelia (PARF_PARTE) Sequence A:  QQVIPAPRVQVTQPYAGQKPGTSGLRKKVSEATQPNYLEN FVQSIFNTLRKDELKPKNVLFVGGDGRYFNRQAIFSIIRL AYANDISEVHVGQAGLMSTPASSHYIRKVNEEVGNCIGGI ILTASHNPGGKEHGDFGIKFNVRTGAPAPEDFTDQIYTHT TKIKEYLTVDYEFEKHINLDQIGVYKFEGTRLEKSHFEVK VVDTVQDYTQLMQKLFDFDLLKGLFSNKDFSFRFDGMHGV AGPYAKHIFGTLLGCSKESLLNCDPSEDFGGGHPDPNLTY AHDLVELLDIHKKKDVGTVPQFGAACDGDADRNMILGRQF FVTPSDSLAVIAANANLIFKNGLLGAARSMPTSGALDKVA AKNGIKLFETPTGWKFFGNLMDAGLINLCGEESFGTGSNH IREKDGIWAVLAWLTILAHKNKNTDHFVTVEEIVTQYWQQ FGRNYYSRYDYEQVDSAGANKMMEHLKTKFQYFEQLKQGN KADIYDYVDPVDQSVSKNQGVRFVFGDGSRIIFRLSGTGS VGATIRIYFEQFEQQQIQHETATALANIIKLGLEISDIAQ FTGRNEPTVIT B:  QQVIPAPRVQVTQPYAGQKPGTSGLRKKVSEATQPNYLEN FVQSIFNTLRKDELKPKNVLFVGGDGRYFNRQAIFSIIRL AYANDISEVHVGQAGLMSTPASSHYIRKVNEEVGNCIGGI ILTASHNPGGKEHGDFGIKFNVRTGAPAPEDFTDQIYTHT TKIKEYLTVDYEFEKHINLDQIGVYKFEGTRLEKSHFEVK VVDTVQDYTQLMQKLFDFDLLKGLFSNKDFSFRFDGMHGV AGPYAKHIFGTLLGCSKESLLNCDPSEDFGGGHPDPNLTY AHDLVELLDIHKKKDVGTVPQFGAACDGDADRNMILGRQF FVTPSDSLAVIAANANLIFKNGLLGAARSMPTSGALDKVA AKNGIKLFETPTGWKFFGNLMDAGLINLCGEESFGTGSNH IREKDGIWAVLAWLTILAHKNKNTDHFVTVEEIVTQYWQQ FGRNYYSRYDYEQVDSAGANKMMEHLKTKFQYFEQLKQGN KADIYDYVDPVDQSVSKNQGVRFVFGDGSRIIFRLSGTGS VGATIRIYFEQFEQQQIQHETATALANIIKLGLEISDIAQ FTGRNEPTVIT Description Functional site 1) chain A residue 126 type sequence S description BINDING SITE FOR RESIDUE CA A 700 source : AC1 2) chain A residue 308 type sequence D description BINDING SITE FOR RESIDUE CA A 700 source : AC1 3) chain A residue 310 type sequence D description BINDING SITE FOR RESIDUE CA A 700 source : AC1 4) chain A residue 312 type sequence D description BINDING SITE FOR RESIDUE CA A 700 source : AC1 5) chain B residue 126 type sequence S description BINDING SITE FOR RESIDUE CA B 700 source : AC2 6) chain B residue 308 type sequence D description BINDING SITE FOR RESIDUE CA B 700 source : AC2 7) chain B residue 310 type sequence D description BINDING SITE FOR RESIDUE CA B 700 source : AC2 8) chain B residue 312 type sequence D description BINDING SITE FOR RESIDUE CA B 700 source : AC2 9) chain A residue 120-129 type prosite sequence GIILTASHNP description PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GIiLTASHNP source prosite : PS00710 10) chain A residue 126 type ACT_SITE sequence S description Phosphoserine intermediate source Swiss-Prot : SWS_FT_FI1 11) chain B residue 126 type ACT_SITE sequence S description Phosphoserine intermediate source Swiss-Prot : SWS_FT_FI1 12) chain A residue 23 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 13) chain B residue 140 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 373 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 392 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 405 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 527 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 27 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 140 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 373 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 392 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 405 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 527 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 24) chain B residue 23 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 27 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 126 type BINDING sequence S description via phosphate group source Swiss-Prot : SWS_FT_FI3 27) chain B residue 126 type BINDING sequence S description via phosphate group source Swiss-Prot : SWS_FT_FI3 28) chain A residue 308 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 29) chain A residue 310 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 30) chain A residue 312 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 31) chain B residue 308 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 32) chain B residue 310 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 33) chain B residue 312 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4

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