[English] 日本語

- EMDB-39779: human phosphorylase kinase alpha/gamma/delta subcomplex - phospho... -
+
Open data
-
Basic information
Entry | ![]() | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | human phosphorylase kinase alpha/gamma/delta subcomplex - phosphorylation and Ca2+ bound state | |||||||||
![]() | EM map | |||||||||
![]() |
| |||||||||
![]() | Kinase / glycogenolysis / CYTOSOLIC PROTEIN | |||||||||
Function / homology | ![]() phosphorylase kinase / phosphorylase kinase activity / phosphorylase kinase complex / transporter inhibitor activity / positive regulation of glycogen catabolic process / tau-protein kinase / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / negative regulation of high voltage-gated calcium channel activity / Glycogen breakdown (glycogenolysis) ...phosphorylase kinase / phosphorylase kinase activity / phosphorylase kinase complex / transporter inhibitor activity / positive regulation of glycogen catabolic process / tau-protein kinase / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / negative regulation of high voltage-gated calcium channel activity / Glycogen breakdown (glycogenolysis) / response to corticosterone / glycogen metabolic process / negative regulation of calcium ion export across plasma membrane / regulation of cardiac muscle cell action potential / presynaptic endocytosis / nitric-oxide synthase binding / regulation of cell communication by electrical coupling involved in cardiac conduction / calcineurin-mediated signaling / regulation of synaptic vesicle exocytosis / protein phosphatase activator activity / adenylate cyclase binding / catalytic complex / regulation of synaptic vesicle endocytosis / detection of calcium ion / regulation of cardiac muscle contraction / postsynaptic cytosol / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / presynaptic cytosol / phosphatidylinositol 3-kinase binding / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / titin binding / sperm midpiece / voltage-gated potassium channel complex / regulation of calcium-mediated signaling / calcium channel complex / substantia nigra development / response to amphetamine / calcium channel regulator activity / regulation of heart rate / nitric-oxide synthase regulator activity / calyx of Held / adenylate cyclase activator activity / sarcomere / regulation of cytokinesis / protein serine/threonine kinase activator activity / generation of precursor metabolites and energy / spindle microtubule / mitochondrial membrane / Schaffer collateral - CA1 synapse / long-term synaptic potentiation / response to calcium ion / spindle pole / calcium-dependent protein binding / G2/M transition of mitotic cell cycle / synaptic vesicle membrane / myelin sheath / growth cone / vesicle / carbohydrate metabolic process / transmembrane transporter binding / calmodulin binding / non-specific serine/threonine protein kinase / G protein-coupled receptor signaling pathway / protein domain specific binding / protein serine kinase activity / calcium ion binding / centrosome / protein kinase binding / enzyme binding / signal transduction / protein-containing complex / ATP binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.52 Å | |||||||||
![]() | Ma R / Yan K | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: Molecular basis for the regulation of human phosphorylase kinase by phosphorylation and Ca2+ Authors: Ma R / Yan K | |||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 398.1 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 18.7 KB 18.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 15.9 KB | Display | ![]() |
Images | ![]() | 23.4 KB | ||
Masks | ![]() | 421.9 MB | ![]() | |
Filedesc metadata | ![]() | 6.9 KB | ||
Others | ![]() ![]() | 391 MB 391 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 946.3 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 945.9 KB | Display | |
Data in XML | ![]() | 25 KB | Display | |
Data in CIF | ![]() | 32.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8z5rMC ![]() 8z5mC ![]() 8z5pC ![]() 8z5qC ![]() 8z5tC M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | EM map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.095 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Mask #1
File | ![]() | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: half map
File | emd_39779_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | half map | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: half map
File | emd_39779_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | half map | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
-Entire : human phosphorylase kinase alpha/gamma/delta subcomplex - phospho...
Entire | Name: human phosphorylase kinase alpha/gamma/delta subcomplex - phosphorylation and Ca2+ bound state |
---|---|
Components |
|
-Supramolecule #1: human phosphorylase kinase alpha/gamma/delta subcomplex - phospho...
Supramolecule | Name: human phosphorylase kinase alpha/gamma/delta subcomplex - phosphorylation and Ca2+ bound state type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 1.3 MDa |
-Macromolecule #1: Phosphorylase b kinase regulatory subunit alpha, skeletal muscle ...
Macromolecule | Name: Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 140.108688 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA YRKNADRDED KAKAYELEQS VVKLMRGLL HCMIRQVDKV E(SEP)FKY(SEP)Q(SEP)TK D(SEP)LHAKYNTK TCATVVGDDQ WGHLQLDATS VYLLF LAQM TASGLHIIHS ...String: MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA YRKNADRDED KAKAYELEQS VVKLMRGLL HCMIRQVDKV E(SEP)FKY(SEP)Q(SEP)TK D(SEP)LHAKYNTK TCATVVGDDQ WGHLQLDATS VYLLF LAQM TASGLHIIHS LDEVNFIQNL VFYIEAAYKT ADFGIWERGD KTNQGISELN AS(SEP)VGMAKAA LEALDELDLF GV KGGPQSV IHVLADEVQH CQ(SEP)ILNSLLP RASTSKEVDA SLLSVVSFPA FAVEDSQLVE LTKQEIITKL QGRYGCCRF LRDGYKTPKE DPNRLYYEPA ELKLFENIEC EWPLFWTYFI LDGVFSGNAE QVQEYKEALE AVLIKGKNGV PLLPELY (SEP)V PPDRVDEEYQ NPHTVDRVPM GKLPHMWGQS LYILGSLMAE GFLAPGEIDP LNRRFSTVPK PDVVVQVSIL AETE EIKTI LKDKGIYVET IAEVYPIRVQ PARIL(SEP)HIYS SLGCNNRMKL SGRPYRHMGV LGTSKLYDIR KTIFTFTPQF I DQQQFYLA LDNKMIVEML RTDL(SEP)YLCSR WRMTGQPTIT FPISHSMLDE DGTSLNSSIL AALRKMQDGY FGGARVQT G KLSEFLTTSC CTHLSFMDPG PEGKLY(SEP)EDY DDNYDYLESG NWMNDYDSTS HARCGDEVAR YLDHLLAH(TPO)A P HPKLAPTS QKGGLDRFQA AVQTTCDLM(SEP) LVTKAKELHV QNVHMYLPTK LFQA(SEP)RP(SEP)FN LLD(SEP)PH PRQ ENQVP(SEP)VRVE IHLPRDQ(SEP)GE VDFKALVLQL KETSSLQEQA DILYMLYTMK GPDWNTELYN ERSATVREL LTELYGKVGE IRHWGLIRYI SGILRKKVEA LDEACTDLLS HQKHL(TPO)VGLP PEPREKTISA PLPYEALTQL IDEASE GDM SISILTQEIM VYLAMYMRTQ PGLFAEMFRL RIGLIIQVMA TELAHSLRCS AEEATEGLMN LSPSAMKNLL HHIL (SEP)GKEF GVER(SEP)VRPTD SNV(SEP)PAI(SEP)IH EIGAVGA(TPO)KT ER(TPO)GIMQLK(SEP) EIKQVEF RR L(SEP)I(SEP)AE(SEP)Q(SEP)P GTSM(TPO)PSSGS FPSAYDQQSS KDSRQGQWQR RRRLDGALNR VPVGFYQK V WKVLQKCHGL SVEGFVLPSS TTREMTPGEI KFSVHVESVL NRVPQPEYRQ LLVEAILVLT MLADIEIHSI GSIIAVEKI VHIANDLFLQ EQKTLGADD(TPO) MLAKDPASGI CTLLYDSAP(SEP) GRFGTMTYLS KAAATYVQEF LPH(SEP)ICAM Q UniProtKB: Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform |
-Macromolecule #2: Phosphorylase b kinase gamma catalytic chain, skeletal muscle/hea...
Macromolecule | Name: Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: phosphorylase kinase |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 45.084672 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MTRDEALPDS HSAQDFYENY EPKEILGRGV SSVVRRCIHK PTSQEYAVKV IDVTGGGSFS PEEVRELREA TLKEVDILRK VSGHPNIIQ LKDTYETNTF FFLVFDLMKR GELFDYLTEK VTLSEKETRK IMRALLEVIC TLHKLNIVHR DLKPENILLD D NMNIKLTD ...String: MTRDEALPDS HSAQDFYENY EPKEILGRGV SSVVRRCIHK PTSQEYAVKV IDVTGGGSFS PEEVRELREA TLKEVDILRK VSGHPNIIQ LKDTYETNTF FFLVFDLMKR GELFDYLTEK VTLSEKETRK IMRALLEVIC TLHKLNIVHR DLKPENILLD D NMNIKLTD FGFSCQLEPG ERLREVCGTP SYLAPEIIEC SMNEDHPGYG KEVDMWSTGV IMYTLLAGSP PFWHRKQMLM LR MIMSGNY QFGSPEWDDY SDTVKDLVSR FLVVQPQNRY TAEEALAHPF FQQYLVEEVR HFSPRGKFKV IALTVLASVR IYY QYRRVK PVTREIVIRD PYALRPLRRL IDAYAFRIYG HWVKKGQQQN RAALFENTPK AVLLSLAEED Y UniProtKB: Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform |
-Macromolecule #3: Calmodulin-3
Macromolecule | Name: Calmodulin-3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 18.921584 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: DYKDDDDKSG PDEVDASGRM ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE E FVQMMTAK UniProtKB: Calmodulin-3 |
-Macromolecule #4: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 1 / Formula: ATP |
---|---|
Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ![]() ChemComp-ATP: |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 6.8 |
---|---|
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |