9s8b

Structure of glycogen phosphorylase - dimeric form - in complex with HPr from Escherichia coli

Method: ELECTRON MICROSCOPY Dmax: 130.1 Å Quality: REASONABLE

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

Glycogen phosphorylase

Escherichia coli

UniProt P0AC86

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–815 Chain B; UniProt 1–815 Non-standard monomer:Yes (specific site not provided by mmCIF) Phosphocarrier protein HPr × 1 (P0AA04) Phosphocarrier protein HPr × 1 (P0AA04) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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.

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

View Construct and Data Evidence
UniProt name PHSG_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 18–832; UniProt 1–815 Author chain B; PDBConstruct 18–832; UniProt 1–815

Phosphocarrier protein HPr

Escherichia coli

UniProt P0AA04

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–85 Chain D; UniProt 1–85 Non-standard monomer:Yes (specific site not provided by mmCIF) Glycogen phosphorylase × 2 (P0AC86) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTHP_ECOLI
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain C; PDBConstruct 18–102; UniProt 1–85 Author chain D; PDBConstruct 18–102; UniProt 1–85

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 9s8b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9s8b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9s8b
Deposition date deposition_date2025-08-05
Structure title titleStructure of glycogen phosphorylase - dimeric form - in complex with HPr from Escherichia coli
Keywords keywordsGlycogen phosphorylase, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.02
Radius of gyration Rg (electron density) rg_electron39.49
Forward intensity I(0) i0587876000.00
Molecular weight molecular_weight198360.0 kDa
Excluded volume excluded_volume247930 ų
Envelope volume envelope_volume309280 ų
Hydration-shell volume shell_volume64435 ų
Envelope diameter envelope_diameter141.5
Shell Rg shell_rg45.63
Envelope Rg envelope_rg39.52
Shape Rg shape_rg39.48
Total Rg total_rg39.83
Total atoms total_atoms14002
Residues n_residues1769
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 dmax130.1
Rg (real space) rg_real39.99
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real5.8790e+08
I(0) uncertainty (real space) i0_real_error1.0100e+07
Rg (reciprocal space) rg_reciprocal40.02
I(0) (reciprocal space) i0_reciprocal587900000.0000
Solution quality estimate total_estimate0.6673
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.4
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.478
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha205100000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 0.025; Positv: 1.000; Valcen: 0.995; Smooth: 0.888

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)