eF-site ID 1kfi-AB PDB Code 1kfi Chain A, B click to enlarge Title Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, pp63/Parafusin (phosphoglucomutase) from Paramecium Classification ISOMERASE Compound phosphoglucomutase 1 Source Paramecium tetraurelia (PARF_PARTE) Sequence A:  QVIPAPRVQVTQPYAGQKPGTSGLRKKVSEATQPNYLENF VQSIFNTLRKDELKPKNVLFVGGDGRYFNRQAIFSIIRLA YANDISEVHVGQAGLMSTPASSHYIRKVNEEVGNCIGGII LTASHNPGGKEHGDFGIKFNVRTGAPAPEDFTDQIYTHTT KIKEYLTVDYEFEKHINLDQIGVYKFEGTRLEKSHFEVKV VDTVQDYTQLMQKLFDFDLLKGLFSNKDFSFRFDGMHGVA GPYAKHIFGTLLGCSKESLLNCDPSEDFGGGHPDPNLTYA HDLVELLDIHKKKDVGTVPQFGAACDGDADRNMILGRQFF VTPSDSLAVIAANANLIFKNGLLGAARSMPTSGALDKVAA KNGIKLFETPTGWKFFGNLMDAGLINLCGEESFGTGSNHI REKDGIWAVLAWLTILAHKNKNTDHFVTVEEIVTQYWQQF GRNYYSRYDYEQVDSAGANKMMEHLKTKFQYFEQLKQGNK ADIYDYVDPVDQSVSKNQGVRFVFGDGSRIIFRLSGTGSV GATIRIYFEQFEQQQIQHETATALANIIKLGLEISDIAQF TGRNEPTVIT B:  QVIPAPRVQVTQPYAGQKPGTSGLRKKVSEATQPNYLENF VQSIFNTLRKDELKPKNVLFVGGDGRYFNRQAIFSIIRLA YANDISEVHVGQAGLMSTPASSHYIRKVNEEVGNCIGGII LTASHNPGGKEHGDFGIKFNVRTGAPAPEDFTDQIYTHTT KIKEYLTVDYEFEKHINLDQIGVYKFEGTRLEKSHFEVKV VDTVQDYTQLMQKLFDFDLLKGLFSNKDFSFRFDGMHGVA GPYAKHIFGTLLGCSKESLLNCDPSEDFGGGHPDPNLTYA HDLVELLDIHKKKDVGTVPQFGAACDGDADRNMILGRQFF VTPSDSLAVIAANANLIFKNGLLGAARSMPTSGALDKVAA KNGIKLFETPTGWKFFGNLMDAGLINLCGEESFGTGSNHI REKDGIWAVLAWLTILAHKNKNTDHFVTVEEIVTQYWQQF GRNYYSRYDYEQVDSAGANKMMEHLKTKFQYFEQLKQGNK ADIYDYVDPVDQSVSKNQGVRFVFGDGSRIIFRLSGTGSV GATIRIYFEQFEQQQIQHETATALANIIKLGLEISDIAQF TGRNEPTVIT Description Functional site 1) chain A residue 308 type sequence D description BINDING SITE FOR RESIDUE ZN A 700 source : AC1 2) chain A residue 310 type sequence D description BINDING SITE FOR RESIDUE ZN A 700 source : AC1 3) chain A residue 312 type sequence D description BINDING SITE FOR RESIDUE ZN A 700 source : AC1 4) chain A residue 126 type sequence S description BINDING SITE FOR RESIDUE SO4 A 601 source : AC2 5) chain A residue 127 type sequence H description BINDING SITE FOR RESIDUE SO4 A 601 source : AC2 6) chain A residue 308 type sequence D description BINDING SITE FOR RESIDUE SO4 A 601 source : AC2 7) chain A residue 310 type sequence D description BINDING SITE FOR RESIDUE SO4 A 601 source : AC2 8) chain A residue 312 type sequence D description BINDING SITE FOR RESIDUE SO4 A 601 source : AC2 9) chain A residue 313 type sequence R description BINDING SITE FOR RESIDUE SO4 A 601 source : AC2 10) chain A residue 405 type sequence K description BINDING SITE FOR RESIDUE SO4 A 601 source : AC2 11) chain A residue 23 type sequence T description BINDING SITE FOR RESIDUE SO4 A 603 source : AC3 12) chain A residue 515 type sequence R description BINDING SITE FOR RESIDUE SO4 A 603 source : AC3 13) chain A residue 517 type sequence S description BINDING SITE FOR RESIDUE SO4 A 603 source : AC3 14) chain A residue 518 type sequence G description BINDING SITE FOR RESIDUE SO4 A 603 source : AC3 15) chain A residue 519 type sequence T description BINDING SITE FOR RESIDUE SO4 A 603 source : AC3 16) chain A residue 527 type sequence R description BINDING SITE FOR RESIDUE SO4 A 603 source : AC3 17) chain B residue 308 type sequence D description BINDING SITE FOR RESIDUE ZN B 700 source : AC4 18) chain B residue 310 type sequence D description BINDING SITE FOR RESIDUE ZN B 700 source : AC4 19) chain B residue 312 type sequence D description BINDING SITE FOR RESIDUE ZN B 700 source : AC4 20) chain B residue 126 type sequence S description BINDING SITE FOR RESIDUE SO4 B 602 source : AC5 21) chain B residue 127 type sequence H description BINDING SITE FOR RESIDUE SO4 B 602 source : AC5 22) chain B residue 308 type sequence D description BINDING SITE FOR RESIDUE SO4 B 602 source : AC5 23) chain B residue 312 type sequence D description BINDING SITE FOR RESIDUE SO4 B 602 source : AC5 24) chain B residue 313 type sequence R description BINDING SITE FOR RESIDUE SO4 B 602 source : AC5 25) chain B residue 375 type sequence W description BINDING SITE FOR RESIDUE SO4 B 602 source : AC5 26) chain B residue 515 type sequence R description BINDING SITE FOR RESIDUE SO4 B 604 source : AC6 27) chain B residue 517 type sequence S description BINDING SITE FOR RESIDUE SO4 B 604 source : AC6 28) chain B residue 518 type sequence G description BINDING SITE FOR RESIDUE SO4 B 604 source : AC6 29) chain B residue 519 type sequence T description BINDING SITE FOR RESIDUE SO4 B 604 source : AC6 30) chain B residue 527 type sequence R description BINDING SITE FOR RESIDUE SO4 B 604 source : AC6 31) chain A residue 120-129 type prosite sequence GIILTASHNP description PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GIiLTASHNP source prosite : PS00710 32) chain A residue 126 type ACT_SITE sequence S description Phosphoserine intermediate source Swiss-Prot : SWS_FT_FI1 33) chain B residue 126 type ACT_SITE sequence S description Phosphoserine intermediate source Swiss-Prot : SWS_FT_FI1 34) chain A residue 23 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 140 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 373 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 392 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 405 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 39) chain B residue 527 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 27 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 140 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 373 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 392 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 405 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 527 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 23 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 27 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00949 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 126 type BINDING sequence S description via phosphate group source Swiss-Prot : SWS_FT_FI3 49) chain B residue 126 type BINDING sequence S description via phosphate group source Swiss-Prot : SWS_FT_FI3 50) chain A residue 308 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 51) chain A residue 310 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 52) chain A residue 312 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 53) chain B residue 308 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 54) chain B residue 310 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 55) chain B residue 312 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4

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