8z5r

human phosphorylase kinase alpha/gamma/delta subcomplex - phosphorylation and Ca2+ bound state

Method: ELECTRON MICROSCOPY Dmax: 130.4 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform

Homo sapiens

UniProt P46020

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–1223 Non-standard monomer:Yes (specific site not provided by mmCIF) Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform × 1 (Q16816) Calmodulin-3 × 1 (P0DP25) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KPB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1223; UniProt 1–1223

Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform

Homo sapiens

UniProt Q16816

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–387 Not recorded Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform × 1 (P46020) Calmodulin-3 × 1 (P0DP25) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHKG1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–387; UniProt 1–387

Calmodulin-3

Homo sapiens

UniProt P0DP25

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–149 Not recorded Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform × 1 (P46020) Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform × 1 (Q16816) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 20–168; UniProt 1–149

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8z5r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8z5r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8z5r
Deposition date deposition_date2024-04-18
Structure title titlehuman phosphorylase kinase alpha/gamma/delta subcomplex - phosphorylation and Ca2+ bound state
Keywords keywordsKinase, glycogenolysis, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier38.91
Radius of gyration Rg (electron density) rg_electron38.19
Forward intensity I(0) i0388973000.00
Molecular weight molecular_weight160350.0 kDa
Excluded volume excluded_volume200780 ų
Envelope volume envelope_volume284510 ų
Hydration-shell volume shell_volume60732 ų
Envelope diameter envelope_diameter139.6
Shell Rg shell_rg45.23
Envelope Rg envelope_rg37.96
Shape Rg shape_rg38.21
Total Rg total_rg38.56
Total atoms total_atoms11273
Residues n_residues1448
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax130.4
Rg (real space) rg_real38.76
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real3.8900e+08
I(0) uncertainty (real space) i0_real_error6.7090e+06
Rg (reciprocal space) rg_reciprocal38.86
I(0) (reciprocal space) i0_reciprocal389000000.0000
Solution quality estimate total_estimate0.8872
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.7
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha102000000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)