7onf

The binding of p-coumaroyl glucose to glycogen phosphorylase reveals the relationship between structural data and effects on cell metabolome

Method: X-RAY DIFFRACTION Dmax: 90.4 Å Quality: GOOD

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

Glycogen phosphorylase, muscle form

OrganismNot specified

UniProt P00489

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 13–837 Not recorded PLP PYRIDOXAL-5'-PHOSPHATE × 2 IMP INOSINIC ACID × 2 VKK p-coumaroyl glucose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:SMALL TUBES;pH 6.8;289 K;10 mM BES buffer Resolution 1.60 Å R-free 0.161

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.

229 other PDB entries and 261 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PYGM_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–825; UniProt 13–837

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 7onf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7onf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7onf
Deposition date deposition_date2021-05-25
Structure title titleThe binding of p-coumaroyl glucose to glycogen phosphorylase reveals the relationship between structural data and effects on cell metabolome
Keywords keywordsTRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.44
Radius of gyration Rg (electron density) rg_electron27.37
Forward intensity I(0) i0140884000.00
Molecular weight molecular_weight94316.0 kDa
Excluded volume excluded_volume118220 ų
Envelope volume envelope_volume139920 ų
Hydration-shell volume shell_volume40809 ų
Envelope diameter envelope_diameter96.7
Shell Rg shell_rg36.28
Envelope Rg envelope_rg27.71
Shape Rg shape_rg27.37
Total Rg total_rg28.18
Total atoms total_atoms6650
Residues n_residues810
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 dmax90.4
Rg (real space) rg_real28.27
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real1.4090e+08
I(0) uncertainty (real space) i0_real_error2.2220e+06
Rg (reciprocal space) rg_reciprocal28.33
I(0) (reciprocal space) i0_reciprocal140900000.0000
Solution quality estimate total_estimate0.8943
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.9
Skewness Skewness skewness0.198
Kurtosis Kurtosis kurtosis-0.476
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha39520000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7onfA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
Domain ID domain_id7onfA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;

8. Citations (1)

9. Files and Curves (10)