1jse

FULL-MATRIX LEAST-SQUARES REFINEMENT OF TURKEY LYSOZYME

Method: X-RAY DIFFRACTION Dmax: 50.4 Å Quality: GOOD

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

LYSOZYME

OrganismNot specified

UniProt P00703

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 POL N-PROPANOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.2;2.2M AMMONIUM SULFATE SOLUTION AT PH 4.2 CONTAINING 10% 1-PROPANOL AND 4% PROTEIN Resolution 1.12 Å R-free 0.140

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.

12 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYSC_MELGA
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 1jse

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jse
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1jse
Deposition date deposition_date1998-01-05
Structure title titleFULL-MATRIX LEAST-SQUARES REFINEMENT OF TURKEY LYSOZYME
Keywords keywordsHYDROLASE, O-GLYCOSYL, TURKEY LYSOZYME, ENZYME; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.21
Radius of gyration Rg (electron density) rg_electron13.95
Forward intensity I(0) i04547470.00
Molecular weight molecular_weight14278.0 kDa
Excluded volume excluded_volume17456 ų
Envelope volume envelope_volume19400 ų
Hydration-shell volume shell_volume11961 ų
Envelope diameter envelope_diameter51.3
Shell Rg shell_rg19.46
Envelope Rg envelope_rg14.23
Shape Rg shape_rg13.94
Total Rg total_rg15.03
Total atoms total_atoms998
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 dmax50.4
Rg (real space) rg_real15.14
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real4.5470e+06
I(0) uncertainty (real space) i0_real_error4.8840e+04
Rg (reciprocal space) rg_reciprocal15.15
I(0) (reciprocal space) i0_reciprocal4547000.0000
Solution quality estimate total_estimate0.8787
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.8
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-0.249
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha759600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1jsea_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.2 — C-type lysozyme

CATH v4.4 (1 domains)

Domain ID domain_id1jseA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)