1xft

Synchrotron X-ray Powder Diffraction Study of Hexagonal Turkey Egg-white Lysozyme

Method: POWDER DIFFRACTION Dmax: 50.3 Å Quality: GOOD

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

Lysozyme C

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 Fragment:LYSOZYME No other associated polymer POWDER DIFFRACTION X-ray crystallization conditions:SALTING OUT;pH 6;295 K;NaCl, pH 6, SALTING OUT, temperature 295K Resolution 3.35 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 1xft

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1xft
Deposition date deposition_date2004-09-15
Structure title titleSynchrotron X-ray Powder Diffraction Study of Hexagonal Turkey Egg-white Lysozyme
Keywords keywordspowder diffraction, lysozyme, x-rays, HYDROLASE; HYDROLASE
Experimental Method methodPOWDER DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.24
Radius of gyration Rg (electron density) rg_electron14.00
Forward intensity I(0) i04499590.00
Molecular weight molecular_weight14088.0 kDa
Excluded volume excluded_volume17175 ų
Envelope volume envelope_volume18722 ų
Hydration-shell volume shell_volume11640 ų
Envelope diameter envelope_diameter49.7
Shell Rg shell_rg19.49
Envelope Rg envelope_rg14.24
Shape Rg shape_rg13.98
Total Rg total_rg15.09
Total atoms total_atoms985
Residues n_residues128
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_real15.17
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real4.5000e+06
I(0) uncertainty (real space) i0_real_error5.8270e+04
Rg (reciprocal space) rg_reciprocal15.18
I(0) (reciprocal space) i0_reciprocal4500000.0000
Solution quality estimate total_estimate0.8759
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.4
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.228
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha485300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1xfta1
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

8. Citations (5)

9. Files and Curves (10)