9mp9

Mix & Quench Time Resolved Lysozyme - NAG1 Complex (1000 ms)

Method: X-RAY DIFFRACTION Dmax: 52.7 Å Quality: GOOD

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

Lysozyme C

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 1–147 Not recorded NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 1 CL CHLORIDE ION × 4 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:SMALL TUBES;pH 4.6;293 K;0.1 M sodium acetate pH 4.6, 20 % (w/v) sodium chloride, 5 % PEG 4000. NAG1 soaked at 226 mM in 0.1 M sodium acetate pH 4.6 and 17.5 % (w/v) sodium chloride, 5 % (w/v) PEG 4000, and 10 % (w/v) PEG 400 Resolution 1.90 Å R-free 0.220

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 1–147; UniProt 1–147

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 9mp9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mp9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mp9
Deposition date deposition_date2024-12-30
Structure title titleMix & Quench Time Resolved Lysozyme - NAG1 Complex (1000 ms)
Keywords keywordsTime resolved, inhibitor, complex, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.12
Radius of gyration Rg (electron density) rg_electron13.84
Forward intensity I(0) i04926670.00
Molecular weight molecular_weight14690.0 kDa
Excluded volume excluded_volume17828 ų
Envelope volume envelope_volume19407 ų
Hydration-shell volume shell_volume12015 ų
Envelope diameter envelope_diameter52.7
Shell Rg shell_rg19.54
Envelope Rg envelope_rg14.19
Shape Rg shape_rg13.81
Total Rg total_rg14.97
Total atoms total_atoms1020
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 dmax52.7
Rg (real space) rg_real15.05
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real4.9270e+06
I(0) uncertainty (real space) i0_real_error5.9900e+04
Rg (reciprocal space) rg_reciprocal15.06
I(0) (reciprocal space) i0_reciprocal4927000.0000
Solution quality estimate total_estimate0.7776
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.0
Skewness Skewness skewness0.256
Kurtosis Kurtosis kurtosis-0.163
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha892400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.707; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)