7ktu

Cryogenic electron microscopy model of full-length human metavinculin H1'-parallel conformation 1

Method: ELECTRON MICROSCOPY Dmax: 110.8 Å Quality: GOOD

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

metavinculin

Homo sapiens

UniProt P18206

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 1–1134 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris, pH 8.0, 150 mM NaCl, 0.2 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.15 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.

32 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VINC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1134; UniProt 1–1134

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 7ktu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ktu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ktu
Deposition date deposition_date2020-11-24
Structure title titleCryogenic electron microscopy model of full-length human metavinculin H1'-parallel conformation 1
Keywords keywords;actin, adaptor protein, cadherin, cancer, catenin, cell adhesion, cell junction, cell migration, cell signaling, focal adhesions, heart failure, inositol phospholipid, integrin, plasma membrane, skeletal muscle, smooth muscle ;; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.35
Radius of gyration Rg (electron density) rg_electron32.83
Forward intensity I(0) i0196182000.00
Molecular weight molecular_weight108380.0 kDa
Excluded volume excluded_volume134710 ų
Envelope volume envelope_volume178310 ų
Hydration-shell volume shell_volume45468 ų
Envelope diameter envelope_diameter118.7
Shell Rg shell_rg39.27
Envelope Rg envelope_rg32.55
Shape Rg shape_rg32.84
Total Rg total_rg33.30
Total atoms total_atoms7577
Residues n_residues995
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 dmax110.8
Rg (real space) rg_real33.31
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real1.9620e+08
I(0) uncertainty (real space) i0_real_error2.8720e+06
Rg (reciprocal space) rg_reciprocal33.34
I(0) (reciprocal space) i0_reciprocal196200000.0000
Solution quality estimate total_estimate0.8778
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.1
Skewness Skewness skewness0.351
Kurtosis Kurtosis kurtosis-0.157
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18060000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)