7uuw

Cryogenic electron microscopy 3D map of F-actin bound by the Actin Binding Domain of alpha-catenin ortholog, HMP1

Method: ELECTRON MICROSCOPY Dmax: 199.7 Å Quality: GOOD

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

Actin, alpha skeletal muscle

Oryctolagus cuniculus

UniProt P68135

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–377 Chain B; UniProt 1–377 Chain C; UniProt 1–377 Chain D; UniProt 1–377 Chain E; UniProt 1–377 Chain F; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Alpha-catenin-like protein hmp-1 × 6 (P90947) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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.

293 other PDB entries and 353 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–377; UniProt 1–377 Author chain B; PDBConstruct 1–377; UniProt 1–377 Author chain C; PDBConstruct 1–377; UniProt 1–377 Author chain D; PDBConstruct 1–377; UniProt 1–377 Author chain E; PDBConstruct 1–377; UniProt 1–377 Author chain F; PDBConstruct 1–377; UniProt 1–377

Alpha-catenin-like protein hmp-1

Caenorhabditis elegans

UniProt P90947

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain G; UniProt 677–927 Chain H; UniProt 677–927 Chain I; UniProt 677–927 Chain K; UniProt 677–927 Chain L; UniProt 677–927 Chain Z; UniProt 677–927 Not recorded Actin, alpha skeletal muscle × 6 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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.

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

View Construct and Data Evidence
UniProt name HMP1_CAEEL
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–251; UniProt 677–927 Author chain H; PDBConstruct 1–251; UniProt 677–927 Author chain I; PDBConstruct 1–251; UniProt 677–927 Author chain K; PDBConstruct 1–251; UniProt 677–927 Author chain L; PDBConstruct 1–251; UniProt 677–927 Author chain Z; PDBConstruct 1–251; UniProt 677–927

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 7uuw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7uuw
Deposition date deposition_date2022-04-29
Structure title titleCryogenic electron microscopy 3D map of F-actin bound by the Actin Binding Domain of alpha-catenin ortholog, HMP1
Keywords keywordsalpha-catenin, HMP1, Actin Binding Domain, F-actin, F-actin binding protein, cell-cell junction, CELL ADHESION; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.81
Radius of gyration Rg (electron density) rg_electron57.33
Forward intensity I(0) i01817060000.00
Molecular weight molecular_weight355250.0 kDa
Excluded volume excluded_volume444350 ų
Envelope volume envelope_volume622230 ų
Hydration-shell volume shell_volume93424 ų
Envelope diameter envelope_diameter214.5
Shell Rg shell_rg55.75
Envelope Rg envelope_rg57.40
Shape Rg shape_rg57.32
Total Rg total_rg57.31
Total atoms total_atoms24852
Residues n_residues3168
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 dmax199.7
Rg (real space) rg_real57.22
Rg uncertainty (real space) rg_real_error2.43
I(0) (real space) i0_real1.8170e+09
I(0) uncertainty (real space) i0_real_error4.3260e+07
Rg (reciprocal space) rg_reciprocal56.45
I(0) (reciprocal space) i0_reciprocal1815000000.0000
Solution quality estimate total_estimate0.8266
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.0
Skewness Skewness skewness0.551
Kurtosis Kurtosis kurtosis-0.207
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha141000000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.744; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.561

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id7uuwG01
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_id7uuwH01
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_id7uuwI01
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_id7uuwK01
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_id7uuwL01
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_id7uuwZ01
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)