1syq

Human vinculin head domain VH1, residues 1-258, in complex with human talin's vinculin binding site 1, residues 607-636

Method: X-RAY DIFFRACTION Dmax: 99.3 Å Quality: REASONABLE

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

vinculin isoform VCL

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–258 Not recorded Talin 1 × 1 (Q9Y490) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.42 Å R-free 0.236
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–258 Not recorded Talin 1 × 6 (Q9Y490) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.42 Å R-free 0.236
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–258 Not recorded Talin 1 × 6 (Q9Y490) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.42 Å R-free 0.236

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 47 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 7–264; UniProt 1–258

Talin 1

OrganismNot specified

UniProt Q9Y490

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 607–631 Not recorded vinculin isoform VCL × 1 (P18206) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.42 Å R-free 0.236
2 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 607–631 Not recorded vinculin isoform VCL × 6 (P18206) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.42 Å R-free 0.236
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 607–631 Not recorded vinculin isoform VCL × 6 (P18206) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.42 Å R-free 0.236

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TLN1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–25; UniProt 607–631

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 1syq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1syq
Deposition date deposition_date2004-04-01
Structure title titleHuman vinculin head domain VH1, residues 1-258, in complex with human talin's vinculin binding site 1, residues 607-636
Keywords keywordscytoskeleton, vinculin, talin, CELL ADHESION; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.69
Radius of gyration Rg (electron density) rg_electron26.87
Forward intensity I(0) i016820800.00
Molecular weight molecular_weight31419.0 kDa
Excluded volume excluded_volume39534 ų
Envelope volume envelope_volume48269 ų
Hydration-shell volume shell_volume17879 ų
Envelope diameter envelope_diameter104.3
Shell Rg shell_rg29.06
Envelope Rg envelope_rg27.17
Shape Rg shape_rg26.88
Total Rg total_rg27.11
Total atoms total_atoms2199
Residues n_residues284
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 dmax99.3
Rg (real space) rg_real27.26
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real1.6820e+07
I(0) uncertainty (real space) i0_real_error2.6320e+05
Rg (reciprocal space) rg_reciprocal27.08
I(0) (reciprocal space) i0_reciprocal16820000.0000
Solution quality estimate total_estimate0.7136
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.2
Skewness Skewness skewness0.749
Kurtosis Kurtosis kurtosis0.031
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4111000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.425; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.129; Smooth: 0.870

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1syqa1
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.9 — alpha-catenin/vinculin-like
Family Family familya.24.9.1 — alpha-catenin/vinculin
Domain ID domain_idd1syqa2
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.9 — alpha-catenin/vinculin-like
Family Family familya.24.9.1 — alpha-catenin/vinculin
Domain ID domain_idd1syqa3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id1syqA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily230 — Alpha-catenin/vinculin-like
Domain ID domain_id1syqA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily230 — Alpha-catenin/vinculin-like

8. Citations (1)

9. Files and Curves (10)