eF-site ID 4u1r-B PDB Code 4u1r Chain B 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 B:  SAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIYEGY QGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTR EGRLKAACNLLQRGITNLCVIGGDGSLTGANLFRKEWSGL LEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCGTDMT IGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYL ALVSALACGADWVFLPESPPEEGWEEQMCVKLSENRARKK RLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDTRVTI LGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACV VSLNGNHAVRLPLMECVQMTQDVQKAMDERRFQDAVRLRG RSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGAPAAG MNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWT DVGGWTGQGGSILGTKRVLPGKYLEEIATQMRTHSINALL IIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVSNNVP GSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMG GYCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEHLTE KMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFDC RKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEA FTTDDSICVLGISKRNVIFQPVAELKKQTDFEHRIPKEQW WLKLRPLMKILA Description Functional site 1) chain B residue 420 type sequence A description binding site for residue PO4 A 803 source : AC3 2) chain B residue 481 type sequence R description binding site for residue PO4 A 803 source : AC3 3) chain B residue 576 type sequence R description binding site for residue PO4 A 805 source : AC5 4) chain B residue 665 type sequence R description binding site for residue PO4 A 805 source : AC5 5) chain B residue 33 type sequence G description binding site for residue ATP B 801 source : AC6 6) chain B residue 34 type sequence G description binding site for residue ATP B 801 source : AC6 7) chain B residue 64 type sequence Y description binding site for residue ATP B 801 source : AC6 8) chain B residue 97 type sequence R description binding site for residue ATP B 801 source : AC6 9) chain B residue 98 type sequence C description binding site for residue ATP B 801 source : AC6 10) chain B residue 101 type sequence F description binding site for residue ATP B 801 source : AC6 11) chain B residue 102 type sequence R description binding site for residue ATP B 801 source : AC6 12) chain B residue 127 type sequence G description binding site for residue ATP B 801 source : AC6 13) chain B residue 128 type sequence D description binding site for residue ATP B 801 source : AC6 14) chain B residue 129 type sequence G description binding site for residue ATP B 801 source : AC6 15) chain B residue 130 type sequence S description binding site for residue ATP B 801 source : AC6 16) chain B residue 133 type sequence G description binding site for residue ATP B 801 source : AC6 17) chain B residue 177 type sequence D description binding site for residue ATP B 801 source : AC6 18) chain B residue 233 type sequence G description binding site for residue PO4 B 802 source : AC7 19) chain B residue 264 type sequence K description binding site for residue PO4 B 802 source : AC7 20) chain B residue 430 type sequence R description binding site for residue PO4 B 802 source : AC7 21) chain B residue 434 type sequence R description binding site for residue PO4 B 802 source : AC7 22) chain B residue 467 type sequence G description binding site for residue PO4 B 802 source : AC7 23) chain B residue 468 type sequence G description binding site for residue PO4 B 802 source : AC7 24) chain B residue 44 type sequence R description binding site for residue PO4 B 803 source : AC8 25) chain B residue 48 type sequence R description binding site for residue PO4 B 803 source : AC8 26) chain B residue 83 type sequence S description binding site for residue PO4 B 803 source : AC8 27) chain B residue 84 type sequence S description binding site for residue PO4 B 803 source : AC8 28) chain B residue 567 type sequence K description binding site for residue PO4 B 803 source : AC8 29) chain B residue 599 type sequence G description binding site for residue PO4 B 803 source : AC8 30) chain B residue 632 type sequence R description binding site for residue PO4 B 803 source : AC8 31) chain B residue 175 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 97 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 127 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 128 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 210 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 301 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 576 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 665 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 39) chain B residue 34 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 173 type BINDING sequence S description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 41) chain B residue 217 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 42) chain B residue 273 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 43) chain B residue 307 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 44) chain B residue 481 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 45) chain B residue 538 type BINDING sequence T description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 46) chain B residue 583 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 47) chain B residue 639 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 48) chain B residue 671 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 744 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 142 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47860 source Swiss-Prot : SWS_FT_FI4 51) chain B 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 B residue 395 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 53) chain B residue 486 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 54) chain B residue 688 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 55) chain B residue 651 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI7 56) chain B residue 540 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI8

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