2xv5

Human lamin A coil 2B fragment

Method: X-RAY DIFFRACTION Dmax: 92.9 Å Quality: REASONABLE

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

LAMIN-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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 328–398 Chain B; UniProt 328–398 Fragment:HUMAN LAMIN A FRAGMENT, RESIDUES 328-398 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;293 K;73% MPD, 10 MM TRIS-HCL, PH 8.5 AND 100 MM NACL, 293 K Resolution 2.40 Å R-free 0.284

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 41 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 4–74; UniProt 328–398 Author chain B; PDBConstruct 4–74; UniProt 328–398

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 2xv5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2xv5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2xv5
Deposition date deposition_date2010-10-22
Structure title titleHuman lamin A coil 2B fragment
Keywords keywordsSTRUCTURAL PROTEIN, INTERMEDIATE FILAMENTS, NUCLEAR MEMBRANE; LEFT-HANDED COILED COIL, RIGHT-HANDED COILED COIL; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.90
Radius of gyration Rg (electron density) rg_electron24.77
Forward intensity I(0) i04547850.00
Molecular weight molecular_weight14017.0 kDa
Excluded volume excluded_volume16859 ų
Envelope volume envelope_volume25491 ų
Hydration-shell volume shell_volume10511 ų
Envelope diameter envelope_diameter93.4
Shell Rg shell_rg26.70
Envelope Rg envelope_rg26.16
Shape Rg shape_rg24.99
Total Rg total_rg24.49
Total atoms total_atoms950
Residues n_residues106
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 dmax92.9
Rg (real space) rg_real24.60
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real4.5480e+06
I(0) uncertainty (real space) i0_real_error7.6500e+04
Rg (reciprocal space) rg_reciprocal24.44
I(0) (reciprocal space) i0_reciprocal4547000.0000
Solution quality estimate total_estimate0.6879
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.4
Skewness Skewness skewness0.737
Kurtosis Kurtosis kurtosis-0.087
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha245600.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.311; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.026; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2xv5A00
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
Domain ID domain_id2xv5B00
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)