3v4w

Structure of E347K mutant of Lamin

Method: X-RAY DIFFRACTION Dmax: 117.4 Å Quality: REASONABLE

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

Prelamin-A/C

Homo sapiens

UniProt P02545

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 313–386 Fragment:Coil 2b Mutation:E347K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;30% 2-methyl-2,4-pentanediol, 0.1 M Sodium Acetate pH 4.6, 0.2 M Sodium Chloride, VAPOR DIFFUSION, SITTING DROP Resolution 3.70 Å R-free 0.339
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 313–386 Fragment:Coil 2b Mutation:E347K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;30% 2-methyl-2,4-pentanediol, 0.1 M Sodium Acetate pH 4.6, 0.2 M Sodium Chloride, VAPOR DIFFUSION, SITTING DROP Resolution 3.70 Å R-free 0.339

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.

24 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LMNA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–74; UniProt 313–386

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 3v4w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3v4w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3v4w
Deposition date deposition_date2011-12-15
Structure title titleStructure of E347K mutant of Lamin
Keywords keywordsSTRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.72
Radius of gyration Rg (electron density) rg_electron31.72
Forward intensity I(0) i01645830.00
Molecular weight molecular_weight8868.0 kDa
Excluded volume excluded_volume10954 ų
Envelope volume envelope_volume17677 ų
Hydration-shell volume shell_volume6667 ų
Envelope diameter envelope_diameter113.9
Shell Rg shell_rg27.00
Envelope Rg envelope_rg33.04
Shape Rg shape_rg31.79
Total Rg total_rg30.85
Total atoms total_atoms619
Residues n_residues74
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 dmax117.4
Rg (real space) rg_real30.76
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real1.6460e+06
I(0) uncertainty (real space) i0_real_error3.0500e+04
Rg (reciprocal space) rg_reciprocal30.32
I(0) (reciprocal space) i0_reciprocal1645000.0000
Solution quality estimate total_estimate0.5968
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary11.1
Skewness Skewness skewness0.681
Kurtosis Kurtosis kurtosis-0.343
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61590.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.003; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.004; Smooth: 0.741

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3v4wA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170

8. Citations (1)

9. Files and Curves (10)