1ifr

Structure of Lamin A/C Globular Domain

Method: X-RAY DIFFRACTION Dmax: 46.6 Å Quality: GOOD

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 436–552 Fragment:residues 436-552 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;PEG4000, ammonium acetate, DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.40 Å

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 LAMA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–121; UniProt 436–552

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 1ifr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ifr
Deposition date deposition_date2001-04-13
Structure title titleStructure of Lamin A/C Globular Domain
Keywords keywordsimmunoglobulin, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.57
Radius of gyration Rg (electron density) rg_electron13.01
Forward intensity I(0) i03469560.00
Molecular weight molecular_weight12560.0 kDa
Excluded volume excluded_volume15530 ų
Envelope volume envelope_volume17340 ų
Hydration-shell volume shell_volume11289 ų
Envelope diameter envelope_diameter45.4
Shell Rg shell_rg18.90
Envelope Rg envelope_rg13.40
Shape Rg shape_rg12.98
Total Rg total_rg14.36
Total atoms total_atoms884
Residues n_residues113
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 dmax46.6
Rg (real space) rg_real14.47
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real3.4700e+06
I(0) uncertainty (real space) i0_real_error4.0560e+04
Rg (reciprocal space) rg_reciprocal14.48
I(0) (reciprocal space) i0_reciprocal3470000.0000
Solution quality estimate total_estimate0.8865
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.112
Kurtosis Kurtosis kurtosis-0.337
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha583600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ifra1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.16 — Lamin A/C globular tail domain
Family Family familyb.1.16.1 — Lamin A/C globular tail domain
Domain ID domain_idd1ifra2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1ifrA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1260 — Lamin Tail domain

8. Citations (1)

9. Files and Curves (10)