1lzy

X-RAY STRUCTURE OF TURKEY EGG LYSOZYME COMPLEX WITH DI-N-ACETYLCHITOBIOSE. RECOGNITION AND BINDING OF ALPHA-ANOMERIC FORM

Method: X-RAY DIFFRACTION Dmax: 50.3 Å Quality: GOOD

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

TURKEY EGG WHITE LYSOZYME

Meleagris gallopavo

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 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 19–147 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.55 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.

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

View Construct and Data Evidence
UniProt name LYC_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 1lzy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1lzy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1lzy
Deposition date deposition_date1995-01-09
Structure title titleX-RAY STRUCTURE OF TURKEY EGG LYSOZYME COMPLEX WITH DI-N-ACETYLCHITOBIOSE. RECOGNITION AND BINDING OF ALPHA-ANOMERIC FORM
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_guinier15.13
Radius of gyration Rg (electron density) rg_electron13.85
Forward intensity I(0) i04806840.00
Molecular weight molecular_weight14644.0 kDa
Excluded volume excluded_volume17874 ų
Envelope volume envelope_volume19714 ų
Hydration-shell volume shell_volume12133 ų
Envelope diameter envelope_diameter49.9
Shell Rg shell_rg19.64
Envelope Rg envelope_rg14.21
Shape Rg shape_rg13.83
Total Rg total_rg14.98
Total atoms total_atoms1023
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 dmax50.3
Rg (real space) rg_real15.06
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real4.8070e+06
I(0) uncertainty (real space) i0_real_error4.9840e+04
Rg (reciprocal space) rg_reciprocal15.06
I(0) (reciprocal space) i0_reciprocal4807000.0000
Solution quality estimate total_estimate0.8010
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.6
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.219
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha942600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.804; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

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_idd1lzya_
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_id1lzyA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (2)

9. Files and Curves (10)