1x8y

Human lamin coil 2B

Method: X-RAY DIFFRACTION Dmax: 116.9 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 305–387 Fragment:human lamin A fragment (residues 305-387) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;0.7M Na/K tartrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.20 Å R-free 0.305

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 4–86; UniProt 305–387

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 1x8y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1x8y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1x8y
Deposition date deposition_date2004-08-19
Structure title titleHuman lamin coil 2B
Keywords keywordsStructural Protein, Intermediate filament protein; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.04
Radius of gyration Rg (electron density) rg_electron30.79
Forward intensity I(0) i01577450.00
Molecular weight molecular_weight8494.0 kDa
Excluded volume excluded_volume10420 ų
Envelope volume envelope_volume16676 ų
Hydration-shell volume shell_volume6523 ų
Envelope diameter envelope_diameter113.5
Shell Rg shell_rg26.39
Envelope Rg envelope_rg32.14
Shape Rg shape_rg30.92
Total Rg total_rg29.78
Total atoms total_atoms594
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 dmax116.9
Rg (real space) rg_real30.01
Rg uncertainty (real space) rg_real_error1.84
I(0) (real space) i0_real1.5770e+06
I(0) uncertainty (real space) i0_real_error2.6740e+04
Rg (reciprocal space) rg_reciprocal29.59
I(0) (reciprocal space) i0_reciprocal1577000.0000
Solution quality estimate total_estimate0.5984
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary10.6
Skewness Skewness skewness0.701
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57170.0000
Real-space data points n_real_points56
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: 0.002; Smooth: 0.765

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1x8ya_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.20 — Intermediate filament protein, coiled coil region
Family Family familyh.1.20.1 — Intermediate filament protein, coiled coil region

CATH v4.4 (1 domains)

Domain ID domain_id1x8yA00
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)