eF-site ID 4u1r-D PDB Code 4u1r Chain D 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 D:  SAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIYEGY QGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTR EGRLKAACNLLQRGITNLCVIGGDGSLTGANLFRKEWSGL LEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCGTDMT IGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYL ALVSALACGADWVFLPESPPEEGWEEQMCVKLSENRARKK RLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDTRVTI LGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACV VSLNGNHAVRLPLMECVQMTQDVQKAMDERRFQDAVRLRG RSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGAPAAG MNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWT DVGGWTGQGGSILGTKRVLPGKYLEEIATQMRTHSINALL IIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVSNNVP GSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMG GYCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEHLTE KMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFDC RKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEA RTTDDSICVLGISKRNVIFQPVAELKKQTDFEHRIPKEQW WLKLRPLMKILA Description (1)  human platelet phosphofructokinase Functional site 1) chain D residue 420 type sequence A description binding site for residue PO4 C 803 source : AD2 2) chain D residue 481 type sequence R description binding site for residue PO4 C 803 source : AD2 3) chain D residue 671 type sequence H description binding site for residue PO4 C 803 source : AD2 4) chain D residue 576 type sequence R description binding site for residue PO4 C 805 source : AD4 5) chain D residue 665 type sequence R description binding site for residue PO4 C 805 source : AD4 6) chain D residue 33 type sequence G description binding site for residue ATP D 801 source : AD5 7) chain D residue 64 type sequence Y description binding site for residue ATP D 801 source : AD5 8) chain D residue 97 type sequence R description binding site for residue ATP D 801 source : AD5 9) chain D residue 98 type sequence C description binding site for residue ATP D 801 source : AD5 10) chain D residue 101 type sequence F description binding site for residue ATP D 801 source : AD5 11) chain D residue 102 type sequence R description binding site for residue ATP D 801 source : AD5 12) chain D residue 127 type sequence G description binding site for residue ATP D 801 source : AD5 13) chain D residue 128 type sequence D description binding site for residue ATP D 801 source : AD5 14) chain D residue 129 type sequence G description binding site for residue ATP D 801 source : AD5 15) chain D residue 130 type sequence S description binding site for residue ATP D 801 source : AD5 16) chain D residue 175 type sequence D description binding site for residue ATP D 801 source : AD5 17) chain D residue 177 type sequence D description binding site for residue ATP D 801 source : AD5 18) chain D residue 233 type sequence G description binding site for residue PO4 D 802 source : AD6 19) chain D residue 264 type sequence K description binding site for residue PO4 D 802 source : AD6 20) chain D residue 430 type sequence R description binding site for residue PO4 D 802 source : AD6 21) chain D residue 434 type sequence R description binding site for residue PO4 D 802 source : AD6 22) chain D residue 467 type sequence G description binding site for residue PO4 D 802 source : AD6 23) chain D residue 468 type sequence G description binding site for residue PO4 D 802 source : AD6 24) chain D residue 44 type sequence R description binding site for residue PO4 D 803 source : AD7 25) chain D residue 48 type sequence R description binding site for residue PO4 D 803 source : AD7 26) chain D residue 83 type sequence S description binding site for residue PO4 D 803 source : AD7 27) chain D residue 84 type sequence S description binding site for residue PO4 D 803 source : AD7 28) chain D residue 567 type sequence K description binding site for residue PO4 D 803 source : AD7 29) chain D residue 599 type sequence G description binding site for residue PO4 D 803 source : AD7 30) chain D residue 632 type sequence R description binding site for residue PO4 D 803 source : AD7 31) chain D residue 651 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI7 32) chain D residue 540 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 33) chain D residue 175 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI1 34) chain D residue 34 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 35) chain D residue 97 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 36) chain D residue 127 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 37) chain D residue 128 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 38) chain D residue 210 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 39) chain D residue 301 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 40) chain D residue 576 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 41) chain D residue 665 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 42) chain D residue 173 type BINDING sequence S description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 43) chain D residue 217 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 44) chain D residue 273 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 45) chain D residue 307 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 46) chain D residue 481 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 47) chain D residue 538 type BINDING sequence T description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 48) chain D residue 583 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 49) chain D residue 639 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 50) chain D residue 671 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 51) chain D residue 744 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 52) chain D residue 395 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 53) chain D residue 486 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 54) chain D residue 688 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 55) chain D residue 142 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47860 source Swiss-Prot : SWS_FT_FI4 56) chain D 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

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