hPhK gamma-delta subcomplex in inactive state. Determined by electron microscopy at 3.1 Å resolution. Released 3 Apr 2024.
Explore 8XYB in 3D Show helices and sheets RCSB PDB PDBe
8XYB contains 41 α-helices and 24 β-strands across 3 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 | 1053-1058 | 6 | |
| α-helix | 1071-1079 | 9 | |
| β-strand | 1084-1087 | 4 | 1 |
| β-strand | 1090-1093 | 4 | 1 |
| α-helix | 1095-1099 | 5 | |
| α-helix | 1105-1115 | 11 | |
| α-helix | 1121-1140 | 20 | |
| β-strand | 1141 | 1 | 2 |
| β-strand | 1148-1150 | 3 | 1 |
| α-helix | 1151-1169 | 19 | |
| α-helix | 1177 | 1 | |
| β-strand | 1178 | 1 | 3 |
| α-helix | 1179 | 1 | |
| β-strand | 1185 | 1 | 3 |
| α-helix | 1186-1190 | 5 | |
| β-strand | 1194 | 1 | 4 |
| α-helix | 1199-1214 | 16 | |
| β-strand | 1220 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-17 | 5 | |
| β-strand | 20-27 | 8 | 6 |
| β-strand | 32-39 | 8 | 6 |
| β-strand | 44-52 | 9 | 6 |
| α-helix | 55-57 | 3 | |
| α-helix | 61-80 | 20 | |
| β-strand | 87 | 1 | 7 |
| β-strand | 92-95 | 4 | 6 |
| β-strand | 99-105 | 7 | 6 |
| β-strand | 111 | 1 | 7 |
| α-helix | 112-118 | 7 | |
| α-helix | 124-143 | 20 | |
| β-strand | 147 | 1 | 8 |
| α-helix | 153-155 | 3 | |
| β-strand | 156-158 | 3 | 7 |
| β-strand | 164-166 | 3 | 7 |
| β-strand | 173 | 1 | 8 |
| α-helix | 174-176 | 3 | |
| β-strand | 181 | 1 | 9 |
| α-helix | 188-190 | 3 | |
| α-helix | 193-200 | 8 | |
| β-strand | 207 | 1 | 9 |
| α-helix | 211-225 | 15 | |
| α-helix | 235-244 | 10 | |
| α-helix | 253-255 | 3 | |
| α-helix | 259-269 | 11 | |
| α-helix | 273-275 | 3 | |
| α-helix | 279-282 | 4 | |
| α-helix | 286-288 | 3 | |
| α-helix | 301-324 | 24 | |
| α-helix | 325-328 | 4 | |
| α-helix | 330-335 | 6 | |
| α-helix | 341-354 | 14 | |
| α-helix | 356-358 | 3 | |
| α-helix | 367-370 | 4 | |
| β-strand | 371 | 1 | 4 |
| α-helix | 376-379 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-20 | 14 | |
| β-strand | 28-29 | 2 | 5 |
| α-helix | 30-39 | 10 | |
| α-helix | 46-57 | 12 | |
| β-strand | 63-64 | 2 | 5 |
| α-helix | 66-73 | 8 | |
| α-helix | 79-93 | 15 | |
| α-helix | 103-113 | 11 | |
| α-helix | 119-129 | 11 | |
| α-helix | 139-147 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform | A | protein | 1223 | Homo sapiens | P46020 (AlphaFold model) |
| Calmodulin-1 | D | protein | 149 | Homo sapiens | P0DP23 (AlphaFold model) |
| Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform | C | protein | 387 | Homo sapiens | Q16816 (AlphaFold model) |
>8XYB_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
>8XYB_2 Calmodulin-1 (chains D) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
>8XYB_3 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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