8cwc

20ns Temperature-Jump (Light) XFEL structure of Lysozyme Bound to N,N'-diacetylchitobiose

Method: X-RAY DIFFRACTION Dmax: 55.9 Å Quality: REASONABLE

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

Lysozyme C

OrganismNot specified

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 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 19–147 Fragment:lyzozyme 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose × 1 NA SODIUM ION × 2 CL CHLORIDE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;pH 3;291 K;Lysozyme-inhibitor complex [20 mg/ml lysozyme plus 10 mg/ml N,N'-diacetylchitobiose dissolved in 0.1 M sodium acetate at pH 3.0] mixed with precipitant [28% (w/v) NaCl, 8% (w/v) PEG6000 and 0.1 M sodium acetate at pH 3.0] in a 1:1 ratio Resolution 1.48 Å R-free 0.169

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 1–129; 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 8cwc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8cwc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8cwc
Deposition date deposition_date2022-05-19
Structure title title20ns Temperature-Jump (Light) XFEL structure of Lysozyme Bound to N,N'-diacetylchitobiose
Keywords keywordslysozyme, temperature-jump, 20ns, light, xfel, HYDROLASE, inhibitor, diacetylchitobiose; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.94
Radius of gyration Rg (electron density) rg_electron13.62
Forward intensity I(0) i05067620.00
Molecular weight molecular_weight14970.0 kDa
Excluded volume excluded_volume18166 ų
Envelope volume envelope_volume18988 ų
Hydration-shell volume shell_volume11864 ų
Envelope diameter envelope_diameter52.6
Shell Rg shell_rg19.47
Envelope Rg envelope_rg14.10
Shape Rg shape_rg13.59
Total Rg total_rg14.77
Total atoms total_atoms2012
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 dmax55.9
Rg (real space) rg_real14.89
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real5.0680e+06
I(0) uncertainty (real space) i0_real_error6.0060e+04
Rg (reciprocal space) rg_reciprocal14.89
I(0) (reciprocal space) i0_reciprocal5068000.0000
Solution quality estimate total_estimate0.7378
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.1
Skewness Skewness skewness0.292
Kurtosis Kurtosis kurtosis-0.096
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha994300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.557; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.916; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8cwcA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (2)

9. Files and Curves (10)