3lyt

COMPARISON OF RADIATION-INDUCED DECAY AND STRUCTURE REFINEMENT FROM X-RAY DATA COLLECTED FROM LYSOZYME CRYSTALS AT LOW AND AMBIENT TEMPERATURES

Method: X-RAY DIFFRACTION Dmax: 73.4 Å Quality: GOOD

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

HEN EGG WHITE LYSOZYME

Gallus gallus

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 mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 19–147 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 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.

1320 other PDB entries and 1449 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 Author chain B; 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 3lyt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3lyt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3lyt
Deposition date deposition_date1992-03-20
Structure title titleCOMPARISON OF RADIATION-INDUCED DECAY AND STRUCTURE REFINEMENT FROM X-RAY DATA COLLECTED FROM LYSOZYME CRYSTALS AT LOW AND AMBIENT TEMPERATURES
Keywords keywordsHYDROLASE(O-GLYCOSYL); HYDROLASE(O-GLYCOSYL)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.10
Radius of gyration Rg (electron density) rg_electron21.43
Forward intensity I(0) i016624000.00
Molecular weight molecular_weight28642.0 kDa
Excluded volume excluded_volume34875 ų
Envelope volume envelope_volume41849 ų
Hydration-shell volume shell_volume17166 ų
Envelope diameter envelope_diameter74.2
Shell Rg shell_rg26.56
Envelope Rg envelope_rg21.39
Shape Rg shape_rg21.42
Total Rg total_rg22.11
Total atoms total_atoms2002
Residues n_residues258
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 dmax73.4
Rg (real space) rg_real22.20
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real1.6620e+07
I(0) uncertainty (real space) i0_real_error2.0970e+05
Rg (reciprocal space) rg_reciprocal22.18
I(0) (reciprocal space) i0_reciprocal16620000.0000
Solution quality estimate total_estimate0.8772
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8
Skewness Skewness skewness0.387
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2525000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.845; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3lyta_
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
Domain ID domain_idd3lytb_
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 (2 domains)

Domain ID domain_id3lytA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10
Domain ID domain_id3lytB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (4)

9. Files and Curves (10)