6rpr

LEM domain of Emerin mutant T43I in complex with BAF dimer and the Igfold of the lamin A/C

Method: X-RAY DIFFRACTION Dmax: 78.7 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 318–433 Not recorded barrier to autointegration factor (BAF) × 2 LEM domain of emerin mutant T43I × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;18% PEG 3350, 100 mM Tris Bis pH 5.5, 0.1 M NH4SO4 Resolution 2.26 Å R-free 0.244

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 P02545-4
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–116; UniProt 318–433

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 6rpr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6rpr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6rpr
Deposition date deposition_date2019-05-14
Structure title titleLEM domain of Emerin mutant T43I in complex with BAF dimer and the Igfold of the lamin A/C
Keywords keywordsNuclear membrane protein, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.32
Radius of gyration Rg (electron density) rg_electron22.35
Forward intensity I(0) i025104800.00
Molecular weight molecular_weight37637.0 kDa
Excluded volume excluded_volume46913 ų
Envelope volume envelope_volume56922 ų
Hydration-shell volume shell_volume21864 ų
Envelope diameter envelope_diameter80.1
Shell Rg shell_rg28.65
Envelope Rg envelope_rg22.64
Shape Rg shape_rg22.34
Total Rg total_rg23.22
Total atoms total_atoms2654
Residues n_residues333
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 dmax78.7
Rg (real space) rg_real23.33
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real2.5100e+07
I(0) uncertainty (real space) i0_real_error3.5630e+05
Rg (reciprocal space) rg_reciprocal23.33
I(0) (reciprocal space) i0_reciprocal25100000.0000
Solution quality estimate total_estimate0.8824
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.363
Kurtosis Kurtosis kurtosis-0.264
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6811000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.971

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd6rprb_
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_idd6rprd_
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.5 — Barrier-to-autointegration factor, BAF
Family Family familya.60.5.1 — Barrier-to-autointegration factor, BAF
Domain ID domain_idd6rpre_
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.5 — Barrier-to-autointegration factor, BAF
Family Family familya.60.5.1 — Barrier-to-autointegration factor, BAF
Domain ID domain_idd6rprg_
Class classa — All alpha proteins
Fold Fold folda.140 — LEM/SAP HeH motif
Superfamily Superfamily superfamilya.140.1 — LEM domain
Family Family familya.140.1.1 — LEM domain

CATH v4.4 (4 domains)

Domain ID domain_id6rprB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1260 — Lamin Tail domain
Domain ID domain_id6rprD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily40 — Barrier-to-autointegration factor, BAF
Domain ID domain_id6rprE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily40 — Barrier-to-autointegration factor, BAF
Domain ID domain_id6rprG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology720 — Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)