8ya1

HEN EGG WHITE LYSOZYME

Method: X-RAY DIFFRACTION Dmax: 52.2 Å Quality: GOOD

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

Lysozyme C

OrganismNot specified

UniProt P00698

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 19–147 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;300 K;0.1 M sodium acetate, 6% sodium chloride Resolution 1.57 Å R-free 0.213

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.

1320 other PDB entries and 1450 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYSC_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–129; UniProt 19–147

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 8ya1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ya1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ya1
Deposition date deposition_date2024-02-07
Structure title titleHEN EGG WHITE LYSOZYME
Keywords keywordsLYSOZYME, HEN EGG WHITE, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.18
Radius of gyration Rg (electron density) rg_electron13.90
Forward intensity I(0) i04687220.00
Molecular weight molecular_weight14321.0 kDa
Excluded volume excluded_volume17437 ų
Envelope volume envelope_volume19210 ų
Hydration-shell volume shell_volume11866 ų
Envelope diameter envelope_diameter52.5
Shell Rg shell_rg19.54
Envelope Rg envelope_rg14.29
Shape Rg shape_rg13.87
Total Rg total_rg15.04
Total atoms total_atoms1001
Residues n_residues129
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 dmax52.2
Rg (real space) rg_real15.12
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real4.6870e+06
I(0) uncertainty (real space) i0_real_error5.7130e+04
Rg (reciprocal space) rg_reciprocal15.12
I(0) (reciprocal space) i0_reciprocal4687000.0000
Solution quality estimate total_estimate0.7803
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.8
Skewness Skewness skewness0.270
Kurtosis Kurtosis kurtosis-0.132
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha784000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.720; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)