3p64

Time-dependent and Protein-directed In Situ Growth of Gold Nanoparticles in a Single Crystal of Lysozyme

Method: X-RAY DIFFRACTION Dmax: 53.2 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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 19–147 Not recorded AU3 GOLD 3+ ION × 3 AU GOLD ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 4.5;298 K;6.5% NaCl (w/v) in 0.1 M sodium acetate, pH 4.5, EVAPORATION, temperature 298K Resolution 1.30 Å R-free 0.234

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 3p64

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3p64
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3p64
Deposition date deposition_date2010-10-11
Structure title titleTime-dependent and Protein-directed In Situ Growth of Gold Nanoparticles in a Single Crystal of Lysozyme
Keywords keywordsHydrolase, Bio-Nano Hybrids, Gold Nanoparticles, Porous Materials; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.33
Radius of gyration Rg (electron density) rg_electron14.00
Forward intensity I(0) i05926010.00
Molecular weight molecular_weight15145.0 kDa
Excluded volume excluded_volume17624 ų
Envelope volume envelope_volume19184 ų
Hydration-shell volume shell_volume11873 ų
Envelope diameter envelope_diameter53.0
Shell Rg shell_rg19.52
Envelope Rg envelope_rg14.22
Shape Rg shape_rg13.89
Total Rg total_rg15.17
Total atoms total_atoms1006
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 dmax53.2
Rg (real space) rg_real15.26
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real5.9260e+06
I(0) uncertainty (real space) i0_real_error7.8830e+04
Rg (reciprocal space) rg_reciprocal15.26
I(0) (reciprocal space) i0_reciprocal5926000.0000
Solution quality estimate total_estimate0.6372
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.199
Kurtosis Kurtosis kurtosis-0.222
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha463500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.731; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.985; 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_idd3p64a_
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_id3p64A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)