eF-site ID 3o8n-AB PDB Code 3o8n Chain A, B click to enlarge Title Structure of phosphofructokinase from rabbit skeletal muscle Classification TRANSFERASE Compound 6-phosphofructokinase, muscle type Source Oryctolagus cuniculus (Rabbit) (K6PF_RABIT) Sequence A:  ARTLGVGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARV FFVHEGYQGLVDGGDHIREATWESVSMMLQLGGTVIGSAR CKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTF RSEWSDLLSDLQKAGKITAEEATRSSYLNIVGLVGSIDND FCGTDMTIGTDSALHRITEIVDAITTTAQSHQRTFVLEVM GRHCGYLALVTSLSCGADWVFIPECPPDDNWEDHLCRRLS ETRTRGSRLNIIIVAEGAIDRNGKPITSEGVKDLVVRRLG YDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGT PDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKRFD EAMKLRGRSFMNNWEVYKLLAHIRPPAPKSGSYTVAVMNV GAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGPAKGQI EEAGWSYVGGWTGQGGSKLGSKRTLPKKSFEQISANITKF NIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPAT VSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVF IIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQAN VEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEG KGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMA GKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELQN QTDFEHRIPKEQWWLKLRPILKILAKYE B:  ARTLGVGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARV FFVHEGYQGLVDGGDHIREATWESVSMMLQLGGTVIGSAR CKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTF RSEWSDLLSDLQKAGKITAEEATRSSYLNIVGLVGSIDND FCGTDMTIGTDSALHRITEIVDAITTTAQSHQRTFVLEVM GRHCGYLALVTSLSCGADWVFIPECPPDDNWEDHLCRRLS ETRTRGSRLNIIIVAEGAIDRNGKPITSEGVKDLVVRRLG YDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGT PDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKRFD EAMKLRGRSFMNNWEVYKLLAHIRPPAPKSGSYTVAVMNV GAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGPAKGQI EEAGWSYVGGWTGQGGSKLGSKRTLPKKSFEQISANITKF NIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPAT VSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVF IIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQAN VEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEG KGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMA GKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELQN QTDFEHRIPKEQWWLKLRPILKILAKYE Description Functional site 1) chain A residue 23 type sequence S description BINDING SITE FOR RESIDUE ADP A 763 source : AC1 2) chain A residue 24 type sequence G description BINDING SITE FOR RESIDUE ADP A 763 source : AC1 3) chain A residue 55 type sequence Y description BINDING SITE FOR RESIDUE ADP A 763 source : AC1 4) chain A residue 88 type sequence R description BINDING SITE FOR RESIDUE ADP A 763 source : AC1 5) chain A residue 89 type sequence C description BINDING SITE FOR RESIDUE ADP A 763 source : AC1 6) chain A residue 93 type sequence R description BINDING SITE FOR RESIDUE ADP A 763 source : AC1 7) chain A residue 118 type sequence G description BINDING SITE FOR RESIDUE ADP A 763 source : AC1 8) chain A residue 119 type sequence D description BINDING SITE FOR RESIDUE ADP A 763 source : AC1 9) chain A residue 120 type sequence G description BINDING SITE FOR RESIDUE ADP A 763 source : AC1 10) chain A residue 121 type sequence S description BINDING SITE FOR RESIDUE ADP A 763 source : AC1 11) chain A residue 124 type sequence G description BINDING SITE FOR RESIDUE ADP A 763 source : AC1 12) chain A residue 173 type sequence D description BINDING SITE FOR RESIDUE ADP A 764 source : AC2 13) chain A residue 174 type sequence M description BINDING SITE FOR RESIDUE ADP A 764 source : AC2 14) chain A residue 179 type sequence D description BINDING SITE FOR RESIDUE ADP A 764 source : AC2 15) chain A residue 214 type sequence Y description BINDING SITE FOR RESIDUE ADP A 764 source : AC2 16) chain A residue 308 type sequence F description BINDING SITE FOR RESIDUE ADP A 764 source : AC2 17) chain A residue 377 type sequence S description BINDING SITE FOR RESIDUE ADP A 764 source : AC2 18) chain A residue 381 type sequence N description BINDING SITE FOR RESIDUE ADP A 764 source : AC2 19) chain A residue 543 type sequence D description BINDING SITE FOR RESIDUE ADP A 764 source : AC2 20) chain A residue 671 type sequence F description BINDING SITE FOR RESIDUE ADP A 764 source : AC2 21) chain A residue 227 type sequence W description BINDING SITE FOR RESIDUE ADP A 765 source : AC3 22) chain A residue 228 type sequence V description BINDING SITE FOR RESIDUE ADP A 765 source : AC3 23) chain A residue 242 type sequence H description BINDING SITE FOR RESIDUE ADP A 765 source : AC3 24) chain A residue 246 type sequence R description BINDING SITE FOR RESIDUE ADP A 765 source : AC3 25) chain A residue 385 type sequence Y description BINDING SITE FOR RESIDUE ADP A 765 source : AC3 26) chain A residue 386 type sequence K description BINDING SITE FOR RESIDUE ADP A 765 source : AC3 27) chain B residue 24 type sequence G description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 28) chain B residue 55 type sequence Y description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 29) chain B residue 88 type sequence R description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 30) chain B residue 89 type sequence C description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 31) chain B residue 92 type sequence F description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 32) chain B residue 93 type sequence R description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 33) chain B residue 118 type sequence G description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 34) chain B residue 119 type sequence D description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 35) chain B residue 120 type sequence G description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 36) chain B residue 121 type sequence S description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 37) chain B residue 123 type sequence T description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 38) chain B residue 124 type sequence G description BINDING SITE FOR RESIDUE ADP B 763 source : AC4 39) chain B residue 173 type sequence D description BINDING SITE FOR RESIDUE ADP B 764 source : AC5 40) chain B residue 174 type sequence M description BINDING SITE FOR RESIDUE ADP B 764 source : AC5 41) chain B residue 214 type sequence Y description BINDING SITE FOR RESIDUE ADP B 764 source : AC5 42) chain B residue 308 type sequence F description BINDING SITE FOR RESIDUE ADP B 764 source : AC5 43) chain B residue 341 type sequence N description BINDING SITE FOR RESIDUE ADP B 764 source : AC5 44) chain B residue 377 type sequence S description BINDING SITE FOR RESIDUE ADP B 764 source : AC5 45) chain B residue 381 type sequence N description BINDING SITE FOR RESIDUE ADP B 764 source : AC5 46) chain B residue 543 type sequence D description BINDING SITE FOR RESIDUE ADP B 764 source : AC5 47) chain B residue 671 type sequence F description BINDING SITE FOR RESIDUE ADP B 764 source : AC5 48) chain B residue 678 type sequence K description BINDING SITE FOR RESIDUE ADP B 764 source : AC5 49) chain B residue 713 type sequence M description BINDING SITE FOR RESIDUE ADP B 764 source : AC5 50) chain B residue 227 type sequence W description BINDING SITE FOR RESIDUE ADP B 765 source : AC6 51) chain B residue 228 type sequence V description BINDING SITE FOR RESIDUE ADP B 765 source : AC6 52) chain B residue 242 type sequence H description BINDING SITE FOR RESIDUE ADP B 765 source : AC6 53) chain B residue 246 type sequence R description BINDING SITE FOR RESIDUE ADP B 765 source : AC6 54) chain B residue 382 type sequence W description BINDING SITE FOR RESIDUE ADP B 765 source : AC6 55) chain B residue 385 type sequence Y description BINDING SITE FOR RESIDUE ADP B 765 source : AC6 56) chain B residue 386 type sequence K description BINDING SITE FOR RESIDUE ADP B 765 source : AC6 57) chain B residue 389 type sequence A description BINDING SITE FOR RESIDUE ADP B 765 source : AC6 58) chain A residue 35 type sequence R description BINDING SITE FOR RESIDUE PO4 A 766 source : AC7 59) chain A residue 39 type sequence R description BINDING SITE FOR RESIDUE PO4 A 766 source : AC7 60) chain A residue 74 type sequence S description BINDING SITE FOR RESIDUE PO4 A 766 source : AC7 61) chain A residue 589 type sequence G description BINDING SITE FOR RESIDUE PO4 A 766 source : AC7 62) chain A residue 420 type sequence R description BINDING SITE FOR RESIDUE PO4 A 767 source : AC8 63) chain A residue 424 type sequence R description BINDING SITE FOR RESIDUE PO4 A 767 source : AC8 64) chain A residue 457 type sequence G description BINDING SITE FOR RESIDUE PO4 A 767 source : AC8 65) chain A residue 458 type sequence G description BINDING SITE FOR RESIDUE PO4 A 767 source : AC8 66) chain A residue 471 type sequence R description BINDING SITE FOR RESIDUE PO4 A 768 source : AC9 67) chain A residue 528 type sequence T description BINDING SITE FOR RESIDUE PO4 A 768 source : AC9 68) chain A residue 530 type sequence S description BINDING SITE FOR RESIDUE PO4 A 768 source : AC9 69) chain A residue 532 type sequence N description BINDING SITE FOR RESIDUE PO4 A 768 source : AC9 70) chain A residue 735 type sequence R description BINDING SITE FOR RESIDUE PO4 A 768 source : AC9 71) chain B residue 39 type sequence R description BINDING SITE FOR RESIDUE PO4 B 766 source : BC1 72) chain B residue 74 type sequence S description BINDING SITE FOR RESIDUE PO4 B 766 source : BC1 73) chain B residue 75 type sequence M description BINDING SITE FOR RESIDUE PO4 B 766 source : BC1 74) chain B residue 224 type sequence G description BINDING SITE FOR RESIDUE PO4 B 767 source : BC2 75) chain B residue 420 type sequence R description BINDING SITE FOR RESIDUE PO4 B 767 source : BC2 76) chain B residue 424 type sequence R description BINDING SITE FOR RESIDUE PO4 B 767 source : BC2 77) chain B residue 458 type sequence G description BINDING SITE FOR RESIDUE PO4 B 767 source : BC2 78) chain B residue 471 type sequence R description BINDING SITE FOR RESIDUE PO4 B 768 source : BC3 79) chain B residue 530 type sequence S description BINDING SITE FOR RESIDUE PO4 B 768 source : BC3 80) chain B residue 532 type sequence N description BINDING SITE FOR RESIDUE PO4 B 768 source : BC3 81) chain B residue 735 type sequence R description BINDING SITE FOR RESIDUE PO4 B 768 source : BC3 82) chain A residue 530 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 83) chain B residue 530 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 84) chain A residue 377 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47857 source Swiss-Prot : SWS_FT_FI6 85) chain B residue 377 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47857 source Swiss-Prot : SWS_FT_FI6 86) chain A residue 557 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P08237 source Swiss-Prot : SWS_FT_FI7 87) chain B residue 557 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P08237 source Swiss-Prot : SWS_FT_FI7 88) chain A residue 667 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P08237 source Swiss-Prot : SWS_FT_FI8 89) chain B residue 667 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P08237 source Swiss-Prot : SWS_FT_FI8 90) chain A residue 166 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI1 91) chain B residue 166 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI1 92) chain A residue 25 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 93) chain B residue 88 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 94) chain B residue 118 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 95) chain B residue 119 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 96) chain B residue 201 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 97) chain B residue 292 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 98) chain B residue 566 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 99) chain B residue 655 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 100) chain A residue 88 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 101) chain A residue 118 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 102) chain A residue 119 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 103) chain A residue 201 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 104) chain A residue 292 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 105) chain A residue 566 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 106) chain A residue 655 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 107) chain B residue 25 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 108) chain A residue 164 type BINDING sequence S description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 109) chain A residue 735 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 110) chain B residue 164 type BINDING sequence S description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 111) chain B residue 208 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 112) chain B residue 264 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 113) chain B residue 298 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 114) chain B residue 471 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 115) chain B residue 528 type BINDING sequence T description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 116) chain B residue 573 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 117) chain B residue 629 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 118) chain B residue 661 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 119) chain A residue 208 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 120) chain B residue 735 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 121) chain A residue 264 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 122) chain A residue 298 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 123) chain A residue 471 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 124) chain A residue 528 type BINDING sequence T description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 125) chain A residue 573 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 126) chain A residue 629 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 127) chain A residue 661 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 128) chain A residue 133 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47858 source Swiss-Prot : SWS_FT_FI5 129) chain B residue 133 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47858 source Swiss-Prot : SWS_FT_FI5 130) chain A residue 292-310 type prosite sequence RVTVLGHVQRGGTPSAFDR description PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGtpsafDR source prosite : PS00433 131) chain A residue 655-673 type prosite sequence RKNVLGHMQQGGSPTPFDR description PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGtpsafDR source prosite : PS00433

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