4p2e

Acoustic transfer of protein crystals from agar pedestals to micromeshes for high throughput screening of heavy atom derivatives

Method: X-RAY DIFFRACTION Dmax: 55.4 Å Quality: GOOD

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 19–147 Not recorded NA SODIUM ION × 1 CL CHLORIDE ION × 5 CU COPPER (II) ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;291 K;0.2M sodium acetate pH4.6, 8% sodium chloride Resolution 1.60 Å R-free 0.194

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 4p2e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4p2e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4p2e
Deposition date deposition_date2014-03-03
Structure title titleAcoustic transfer of protein crystals from agar pedestals to micromeshes for high throughput screening of heavy atom derivatives
Keywords keywordsCopper binding, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.60
Radius of gyration Rg (electron density) rg_electron14.13
Forward intensity I(0) i05197490.00
Molecular weight molecular_weight14776.0 kDa
Excluded volume excluded_volume17725 ų
Envelope volume envelope_volume19748 ų
Hydration-shell volume shell_volume12075 ų
Envelope diameter envelope_diameter55.7
Shell Rg shell_rg19.65
Envelope Rg envelope_rg14.44
Shape Rg shape_rg13.94
Total Rg total_rg15.58
Total atoms total_atoms1011
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 dmax55.4
Rg (real space) rg_real15.57
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real5.1970e+06
I(0) uncertainty (real space) i0_real_error6.8160e+04
Rg (reciprocal space) rg_reciprocal15.58
I(0) (reciprocal space) i0_reciprocal5197000.0000
Solution quality estimate total_estimate0.7643
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.4
Skewness Skewness skewness0.359
Kurtosis Kurtosis kurtosis0.095
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha895500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.656; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4p2ea_
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_id4p2eA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)