4nsh

Carboplatin binding to HEWL in 0.2M NH4SO4, 0.1M NaAc in 25% PEG 4000 at pH 4.6

Method: X-RAY DIFFRACTION Dmax: 52.2 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 DMS DIMETHYL SULFOXIDE × 3 ACT ACETATE ION × 3 QPT carboplatin × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;298 K;20mg of HEWL (0.6mM) was dissolved in 1ml distilled water. 1.4mg of carboplatin (1.8mM) was added with 75 l DMSO. 2 l of this mixed with 2 l resevoir soultion 0.2M NH4SO4, 0.1M NaAc in 25% PEG 4000 at pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.10 Å R-free 0.262

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 4nsh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4nsh
Deposition date deposition_date2013-11-28
Structure title titleCarboplatin binding to HEWL in 0.2M NH4SO4, 0.1M NaAc in 25% PEG 4000 at pH 4.6
Keywords keywordsHydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.29
Radius of gyration Rg (electron density) rg_electron13.99
Forward intensity I(0) i05835520.00
Molecular weight molecular_weight15325.0 kDa
Excluded volume excluded_volume18151 ų
Envelope volume envelope_volume19860 ų
Hydration-shell volume shell_volume12156 ų
Envelope diameter envelope_diameter53.2
Shell Rg shell_rg19.65
Envelope Rg envelope_rg14.33
Shape Rg shape_rg13.95
Total Rg total_rg15.08
Total atoms total_atoms1039
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 dmax52.2
Rg (real space) rg_real15.21
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real5.8360e+06
I(0) uncertainty (real space) i0_real_error6.7990e+04
Rg (reciprocal space) rg_reciprocal15.21
I(0) (reciprocal space) i0_reciprocal5836000.0000
Solution quality estimate total_estimate0.7838
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.8
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.138
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha522000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.730; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4nsha_
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_id4nshA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)