hPhK alpha-gamma subcomplex in active state. Determined by electron microscopy at 2.9 Å resolution. Released 3 Apr 2024.
Explore 8XY7 in 3D Show helices and sheets RCSB PDB PDBe
8XY7 contains 59 α-helices and 41 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-21 | 14 | |
| α-helix | 23-25 | 3 | |
| β-strand | 42-43 | 2 | 1 |
| α-helix | 44-50 | 7 | |
| α-helix | 52-62 | 11 | |
| α-helix | 68-93 | 26 | |
| α-helix | 96-104 | 9 | |
| α-helix | 108-110 | 3 | |
| α-helix | 112-113 | 2 | |
| β-strand | 115-116 | 2 | 1 |
| α-helix | 127-129 | 3 | |
| α-helix | 135-149 | 15 | |
| α-helix | 159-171 | 13 | |
| β-strand | 180 | 1 | 2 |
| β-strand | 196 | 1 | 2 |
| α-helix | 199-211 | 13 | |
| α-helix | 232-245 | 14 | |
| β-strand | 250 | 1 | 3 |
| β-strand | 253 | 1 | 3 |
| β-strand | 256 | 1 | 4 |
| α-helix | 257-259 | 3 | |
| α-helix | 260-263 | 4 | |
| α-helix | 273-286 | 14 | |
| β-strand | 288-289 | 2 | 5 |
| β-strand | 292-294 | 3 | 5 |
| β-strand | 296 | 1 | 4 |
| α-helix | 325-326 | 2 | |
| β-strand | 327-328 | 2 | 5 |
| α-helix | 330-337 | 8 | |
| β-strand | 372-374 | 3 | 5 |
| α-helix | 377-379 | 3 | |
| α-helix | 380-385 | 6 | |
| α-helix | 392 | 1 | |
| β-strand | 393-395 | 3 | 5 |
| α-helix | 401-414 | 14 | |
| α-helix | 420-423 | 4 | |
| α-helix | 428-430 | 3 | |
| α-helix | 434-438 | 5 | |
| β-strand | 440-446 | 7 | 6 |
| α-helix | 449-457 | 9 | |
| β-strand | 463-464 | 2 | 6 |
| β-strand | 472-474 | 3 | 7 |
| α-helix | 476-483 | 8 | |
| β-strand | 489 | 1 | 8 |
| β-strand | 494 | 1 | 8 |
| α-helix | 506-508 | 3 | |
| β-strand | 511-513 | 3 | 7 |
| β-strand | 516-520 | 5 | 7 |
| α-helix | 523-526 | 4 | |
| α-helix | 531-533 | 3 | |
| α-helix | 536-553 | 18 | |
| β-strand | 559 | 1 | 9 |
| β-strand | 561-566 | 6 | 6 |
| α-helix | 568-570 | 3 | |
| β-strand | 571 | 1 | 10 |
| β-strand | 578 | 1 | 10 |
| α-helix | 580-590 | 11 | |
| β-strand | 593-594 | 2 | 11 |
| β-strand | 597-598 | 2 | 11 |
| β-strand | 599-601 | 3 | 6 |
| α-helix | 606-608 | 3 | |
| β-strand | 611 | 1 | 9 |
| β-strand | 614-615 | 2 | 7 |
| α-helix | 617-619 | 3 | |
| α-helix | 767-770 | 4 | |
| α-helix | 782-788 | 7 | |
| α-helix | 789-793 | 5 | |
| β-strand | 799 | 1 | 12 |
| β-strand | 805 | 1 | 12 |
| α-helix | 806-820 | 15 | |
| α-helix | 823-832 | 10 | |
| α-helix | 840-849 | 10 | |
| β-strand | 853-855 | 3 | 13 |
| β-strand | 866-867 | 2 | 13 |
| α-helix | 873-883 | 11 | |
| α-helix | 891-907 | 17 | |
| α-helix | 909-912 | 4 | |
| β-strand | 915 | 1 | 14 |
| β-strand | 917-919 | 3 | 13 |
| α-helix | 920-933 | 14 | |
| α-helix | 939-945 | 7 | |
| α-helix | 951-963 | 13 | |
| α-helix | 1053-1063 | 11 | |
| β-strand | 1066 | 1 | 14 |
| α-helix | 1071-1081 | 11 | |
| β-strand | 1084-1087 | 4 | 15 |
| β-strand | 1090-1093 | 4 | 15 |
| α-helix | 1094-1096 | 3 | |
| α-helix | 1107-1114 | 8 | |
| α-helix | 1121-1140 | 20 | |
| β-strand | 1149-1150 | 2 | 15 |
| α-helix | 1151-1169 | 19 | |
| α-helix | 1186-1190 | 5 | |
| β-strand | 1194 | 1 | 16 |
| α-helix | 1199-1207 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 330-335 | 6 | |
| α-helix | 341-355 | 15 | |
| α-helix | 368-370 | 3 | |
| β-strand | 371 | 1 | 16 |
| α-helix | 376-379 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform | A | protein | 1223 | Homo sapiens | P46020 (AlphaFold model) |
| Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform | C | protein | 387 | Homo sapiens | Q16816 (AlphaFold model) |
>8XY7_1 Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform (chains A) MRSRSNSGVRLDGYARLVQQTILCHQNPVTGLLPASYDQKDAWVRDNVYSILAVWGLGLA YRKNADRDEDKAKAYELEQSVVKLMRGLLHCMIRQVDKVESFKYSQSTKDSLHAKYNTKT CATVVGDDQWGHLQLDATSVYLLFLAQMTASGLHIIHSLDEVNFIQNLVFYIEAAYKTAD FGIWERGDKTNQGISELNASSVGMAKAALEALDELDLFGVKGGPQSVIHVLADEVQHCQS ILNSLLPRASTSKEVDASLLSVVSFPAFAVEDSQLVELTKQEIITKLQGRYGCCRFLRDG YKTPKEDPNRLYYEPAELKLFENIECEWPLFWTYFILDGVFSGNAEQVQEYKEALEAVLI KGKNGVPLLPELYSVPPDRVDEEYQNPHTVDRVPMGKLPHMWGQSLYILGSLMAEGFLAP GEIDPLNRRFSTVPKPDVVVQVSILAETEEIKTILKDKGIYVETIAEVYPIRVQPARILS HIYSSLGCNNRMKLSGRPYRHMGVLGTSKLYDIRKTIFTFTPQFIDQQQFYLALDNKMIV EMLRTDLSYLCSRWRMTGQPTITFPISHSMLDEDGTSLNSSILAALRKMQDGYFGGARVQ TGKLSEFLTTSCCTHLSFMDPGPEGKLYSEDYDDNYDYLESGNWMNDYDSTSHARCGDEV ARYLDHLLAHTAPHPKLAPTSQKGGLDRFQAAVQTTCDLMSLVTKAKELHVQNVHMYLPT KLFQASRPSFNLLDSPHPRQENQVPSVRVEIHLPRDQSGEVDFKALVLQLKETSSLQEQA DILYMLYTMKGPDWNTELYNERSATVRELLTELYGKVGEIRHWGLIRYISGILRKKVEAL DEACTDLLSHQKHLTVGLPPEPREKTISAPLPYEALTQLIDEASEGDMSISILTQEIMVY LAMYMRTQPGLFAEMFRLRIGLIIQVMATELAHSLRCSAEEATEGLMNLSPSAMKNLLHH ILSGKEFGVERSVRPTDSNVSPAISIHEIGAVGATKTERTGIMQLKSEIKQVEFRRLSIS AESQSPGTSMTPSSGSFPSAYDQQSSKDSRQGQWQRRRRLDGALNRVPVGFYQKVWKVLQ KCHGLSVEGFVLPSSTTREMTPGEIKFSVHVESVLNRVPQPEYRQLLVEAILVLTMLADI EIHSIGSIIAVEKIVHIANDLFLQEQKTLGADDTMLAKDPASGICTLLYDSAPSGRFGTM TYLSKAAATYVQEFLPHSICAMQ
>8XY7_2 Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (chains C) MTRDEALPDSHSAQDFYENYEPKEILGRGVSSVVRRCIHKPTSQEYAVKVIDVTGGGSFS PEEVRELREATLKEVDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKRGELFDYLTEKV TLSEKETRKIMRALLEVICTLHKLNIVHRDLKPENILLDDNMNIKLTDFGFSCQLEPGER LREVCGTPSYLAPEIIECSMNEDHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLR MIMSGNYQFGSPEWDDYSDTVKDLVSRFLVVQPQNRYTAEEALAHPFFQQYLVEEVRHFS PRGKFKVIALTVLASVRIYYQYRRVKPVTREIVIRDPYALRPLRRLIDAYAFRIYGHWVK KGQQQNRAALFENTPKAVLLSLAEEDY
| ID | Name | Formula | Copies |
|---|---|---|---|
| FAR | Farnesyl | C15 H26 | 1 |
Architecture and activation of human muscle phosphorylase kinase. Yang, X., Zhu, M., Lu, X. et al. Nat Commun (2024) 15:2719-2719. DOI 10.1038/s41467-024-47049-2 · PubMed
Other PDB entries of the same protein (UniProt P46020 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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