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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | human phosphorylase kinase - inactive state | |||||||||
![]() | EM map | |||||||||
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![]() | Kinase / glycogenolysis / SIGNALING PROTEIN / 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 / response to corticosterone ...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 / response to corticosterone / Glycogen breakdown (glycogenolysis) / glycogen metabolic process / negative regulation of calcium ion export across plasma membrane / regulation of cardiac muscle cell action potential / nitric-oxide synthase binding / presynaptic endocytosis / 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 / postsynaptic cytosol / regulation of cardiac muscle contraction / 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 / calcium channel regulator activity / response to amphetamine / nitric-oxide synthase regulator activity / regulation of heart rate / adenylate cyclase activator activity / calyx of Held / protein serine/threonine kinase activator activity / sarcomere / regulation of cytokinesis / 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 / non-specific serine/threonine protein kinase / calmodulin binding / G protein-coupled receptor signaling pathway / protein domain specific binding / protein serine kinase activity / centrosome / calcium ion binding / 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: 3.41 Å | |||||||||
![]() | Ma R / Yan K | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular basis for the regulation of human phosphorylase kinase by phosphorylation and Ca2+ Authors: Ma R / Yan K | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 398.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.2 KB 20.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 15.8 KB | Display | ![]() |
Images | ![]() | 27.4 KB | ||
Masks | ![]() | 421.9 MB | ![]() | |
Filedesc metadata | ![]() | 7.4 KB | ||
Others | ![]() ![]() | 391.3 MB 391.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 934.5 KB | Display | ![]() |
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Full document | ![]() | 934.1 KB | Display | |
Data in XML | ![]() | 25.3 KB | Display | |
Data in CIF | ![]() | 33.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8z5pMC ![]() 8z5mC ![]() 8z5qC ![]() 8z5rC ![]() 8z5tC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | EM map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Half map: half map
File | emd_39777_half_map_1.map | ||||||||||||
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Annotation | half map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map
File | emd_39777_half_map_2.map | ||||||||||||
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Annotation | half map | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : human phosphorylase kinase - inactive state
Entire | Name: human phosphorylase kinase - inactive state |
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Components |
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-Supramolecule #1: human phosphorylase kinase - inactive state
Supramolecule | Name: human phosphorylase kinase - inactive state / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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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: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 137.469422 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA YRKNADRDED KAKAYELEQS VVKLMRGLL HCMIRQVDKV ESFKYSQSTK DSLHAKYNTK TCATVVGDDQ WGHLQLDATS VYLLFLAQMT ASGLHIIHSL D EVNFIQNL ...String: MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA YRKNADRDED KAKAYELEQS VVKLMRGLL HCMIRQVDKV ESFKYSQSTK DSLHAKYNTK TCATVVGDDQ WGHLQLDATS VYLLFLAQMT ASGLHIIHSL D EVNFIQNL VFYIEAAYKT ADFGIWERGD KTNQGISELN ASSVGMAKAA LEALDELDLF GVKGGPQSVI HVLADEVQHC QS ILNSLLP RASTSKEVDA SLLSVVSFPA FAVEDSQLVE LTKQEIITKL QGRYGCCRFL RDGYKTPKED PNRLYYEPAE LKL FENIEC EWPLFWTYFI LDGVFSGNAE QVQEYKEALE AVLIKGKNGV PLLPELYSVP PDRVDEEYQN PHTVDRVPMG KLPH MWGQS LYILGSLMAE GFLAPGEIDP LNRRFSTVPK PDVVVQVSIL AETEEIKTIL KDKGIYVETI AEVYPIRVQP ARILS HIYS SLGCNNRMKL SGRPYRHMGV LGTSKLYDIR KTIFTFTPQF IDQQQFYLAL DNKMIVEMLR TDLSYLCSRW RMTGQP TIT FPISHSMLDE DGTSLNSSIL AALRKMQDGY FGGARVQTGK LSEFLTTSCC THLSFMDPGP EGKLYSEDYD DNYDYLE SG NWMNDYDSTS HARCGDEVAR YLDHLLAHTA PHPKLAPTSQ KGGLDRFQAA VQTTCDLMSL VTKAKELHVQ NVHMYLPT K LFQASRPSFN LLDSPHPRQE NQVPSVRVEI HLPRDQSGEV DFKALVLQLK ETSSLQEQAD ILYMLYTMKG PDWNTELYN ERSATVRELL TELYGKVGEI RHWGLIRYIS GILRKKVEAL DEACTDLLSH QKHLTVGLPP EPREKTISAP LPYEALTQLI DEASEGDMS ISILTQEIMV YLAMYMRTQP GLFAEMFRLR IGLIIQVMAT ELAHSLRCSA EEATEGLMNL SPSAMKNLLH H ILSGKEFG VERSVRPTDS NVSPAISIHE IGAVGATKTE RTGIMQLKSE IKQVEFRRLS ISAESQSPGT SMTPSSGSFP SA YDQQSSK DSRQGQWQRR RRLDGALNRV PVGFYQKVWK VLQKCHGLSV EGFVLPSSTT REMTPGEIKF SVHVESVLNR VPQ PEYRQL LVEAILVLTM LADIEIHSIG SIIAVEKIVH IANDLFLQEQ KTLGADDTML AKDPASGICT LLYDSAPSGR FGTM TYLSK AAATYVQEFL PHSICAMQ UniProtKB: Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform |
-Macromolecule #2: Phosphorylase b kinase regulatory subunit beta
Macromolecule | Name: Phosphorylase b kinase regulatory subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 125.032961 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MAGAAGLTAE VSWKVLERRA RTKRSGSVYE PLKSINLPRP DNETLWDKLD HYYRIVKSTL LLYQSPTTGL FPTKTCGGDQ KAKIQDSLY CAAGAWALAL AYRRIDDDKG RTHELEHSAI KCMRGILYCY MRQADKVQQF KQDPRPTTCL HSVFNVHTGD E LLSYEEYG ...String: MAGAAGLTAE VSWKVLERRA RTKRSGSVYE PLKSINLPRP DNETLWDKLD HYYRIVKSTL LLYQSPTTGL FPTKTCGGDQ KAKIQDSLY CAAGAWALAL AYRRIDDDKG RTHELEHSAI KCMRGILYCY MRQADKVQQF KQDPRPTTCL HSVFNVHTGD E LLSYEEYG HLQINAVSLY LLYLVEMISS GLQIIYNTDE VSFIQNLVFC VERVYRVPDF GVWERGSKYN NGSTELHSSS VG LAKAALE AINGFNLFGN QGCSWSVIFV DLDAHNRNRQ TLCSLLPRES RSHNTDAALL PCISYPAFAL DDEVLFSQTL DKV VRKLKG KYGFKRFLRD GYRTSLEDPN RCYYKPAEIK LFDGIECEFP IFFLYMMIDG VFRGNPKQVQ EYQDLLTPVL HHTT EGYPV VPKYYYVPAD FVEYEKNNPG SQKRFPSNCG RDGKLFLWGQ ALYIIAKLLA DELISPKDID PVQRYVPLKD QRNVS MRFS NQGPLENDLV VHVALIAESQ RLQVFLNTYG IQTQTPQQVE PIQIWPQQEL VKAYLQLGIN EKLGLSGRPD RPIGCL GTS KIYRILGKTV VCYPIIFDLS DFYMSQDVFL LIDDIKNALQ FIKQYWKMHG RPLFLVLIRE DNIRGSRFNP ILDMLAA LK KGIIGGVKVH VDRLQTLISG AVVEQLDFLR ISDTEELPEF KSFEELEPPK HSKVKRQSST PSAPELGQQP DVNISEWK D KPTHEILQKL NDCSCLASQA ILLGILLKRE GPNFITKEGT VSDHIERVYR RAGSQKLWLA VRYGAAFTQK FSSSIAPHI TTFLVHGKQV TLGAFGHEEE VISNPLSPRV IQNIIYYKCN THDEREAVIQ QELVIHIGWI ISNNPELFSG MLKIRIGWII HAMEYELQI RGGDKPALDL YQLSPSEVKQ LLLDILQPQQ NGRCWLNRRQ IDGSLNRTPT GFYDRVWQIL ERTPNGIIVA G KHLPQQPT LSDMTMYEMN FSLLVEDTLG NIDQPQYRQI VVELLMVVSI VLERNPELEF QDKVDLDRLV KEAFNEFQKD QS RLKEIEK QDDMTSFYNT PPLGKRGTCS YLTKAVMNLL LEGEVKPNND DPCLIS UniProtKB: Phosphorylase b kinase regulatory subunit beta |
-Macromolecule #3: 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: 3 / Number of copies: 2 / Enantiomer: LEVO / EC number: phosphorylase kinase |
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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 #4: Calmodulin-3
Macromolecule | Name: Calmodulin-3 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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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 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 6.8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k 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 |