eF-site ID 4u1r-C PDB Code 4u1r Chain C click to enlarge Title ATP-bound structure of human platelet phosphofructokinase in an R-state, crystal form II Classification TRANSFERASE Compound ATP-dependent 6-phosphofructokinase, platelet type Source Homo sapiens (Human) (PFKAP_HUMAN) Sequence C:  SAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIYEGY QGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTR EGRLKAACNLLQRGITNLCVIGGDGSLTGANLFRKEWSGL LEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCGTDMT IGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYL ALVSALACGADWVFLPESPPEEGWEEQMCVKLSENRARKK RLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDTRVTI LGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACV VSLNGNHAVRLPLMECVQMTQDVQKAMDERRFQDAVRLRG RSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGAPAAG MNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWT DVGGWTGQGGSILGTKRVLPGKYLEEIATQMRTHSINALL IIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVSNNVP GSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMG GYCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEHLTE KMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFDC RKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEA FTTDDSICVLGISKRNVIFQPVAELKKQTDFEHRIPKEQW WLKLRPLMKILA Description (1)  human platelet phosphofructokinase Functional site 1) chain C residue 32 type sequence S description binding site for residue ATP C 801 source : AC9 2) chain C residue 34 type sequence G description binding site for residue ATP C 801 source : AC9 3) chain C residue 64 type sequence Y description binding site for residue ATP C 801 source : AC9 4) chain C residue 97 type sequence R description binding site for residue ATP C 801 source : AC9 5) chain C residue 98 type sequence C description binding site for residue ATP C 801 source : AC9 6) chain C residue 101 type sequence F description binding site for residue ATP C 801 source : AC9 7) chain C residue 102 type sequence R description binding site for residue ATP C 801 source : AC9 8) chain C residue 127 type sequence G description binding site for residue ATP C 801 source : AC9 9) chain C residue 128 type sequence D description binding site for residue ATP C 801 source : AC9 10) chain C residue 129 type sequence G description binding site for residue ATP C 801 source : AC9 11) chain C residue 130 type sequence S description binding site for residue ATP C 801 source : AC9 12) chain C residue 133 type sequence G description binding site for residue ATP C 801 source : AC9 13) chain C residue 233 type sequence G description binding site for residue PO4 C 802 source : AD1 14) chain C residue 264 type sequence K description binding site for residue PO4 C 802 source : AD1 15) chain C residue 430 type sequence R description binding site for residue PO4 C 802 source : AD1 16) chain C residue 434 type sequence R description binding site for residue PO4 C 802 source : AD1 17) chain C residue 467 type sequence G description binding site for residue PO4 C 802 source : AD1 18) chain C residue 468 type sequence G description binding site for residue PO4 C 802 source : AD1 19) chain C residue 665 type sequence R description binding site for residue PO4 C 803 source : AD2 20) chain C residue 44 type sequence R description binding site for residue PO4 C 804 source : AD3 21) chain C residue 48 type sequence R description binding site for residue PO4 C 804 source : AD3 22) chain C residue 83 type sequence S description binding site for residue PO4 C 804 source : AD3 23) chain C residue 84 type sequence S description binding site for residue PO4 C 804 source : AD3 24) chain C residue 599 type sequence G description binding site for residue PO4 C 804 source : AD3 25) chain C residue 632 type sequence R description binding site for residue PO4 C 804 source : AD3 26) chain C residue 481 type sequence R description binding site for residue PO4 C 805 source : AD4 27) chain C residue 671 type sequence H description binding site for residue PO4 C 805 source : AD4 28) chain C residue 175 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI1 29) chain C residue 34 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 30) chain C residue 97 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 31) chain C residue 127 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 32) chain C residue 128 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 33) chain C residue 210 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 34) chain C residue 301 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 35) chain C residue 576 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 36) chain C residue 665 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 37) chain C residue 173 type BINDING sequence S description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 38) chain C residue 217 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 39) chain C residue 273 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 40) chain C residue 307 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 41) chain C residue 481 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 42) chain C residue 538 type BINDING sequence T description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 43) chain C residue 583 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 44) chain C residue 639 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 45) chain C residue 671 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 46) chain C residue 744 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 47) chain C residue 142 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47860 source Swiss-Prot : SWS_FT_FI4 48) chain C residue 395 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 49) chain C residue 486 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 50) chain C residue 688 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 51) chain C residue 386 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:33607258, ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 52) chain C residue 651 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI7 53) chain C residue 540 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI8

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