8ru2

Structure of the F-actin barbed end bound by formin mDia1

Method: ELECTRON MICROSCOPY Dmax: 148.5 Å Quality: GOOD

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

Actin, cytoplasmic 1, N-terminally processed

Homo sapiens

UniProt P60709

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 2–375 Chain C; UniProt 2–375 Chain D; UniProt 2–375 Non-standard monomer:Yes (specific site not provided by mmCIF) Methylated-DNA--protein-cysteine methyltransferase,Protein diaphanous homolog 1 × 2 (P16455,O08808) ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;3 seconds, force 0. Resolution 3.49 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.

72 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–374; UniProt 2–375 Author chain C; PDBConstruct 1–374; UniProt 2–375 Author chain D; PDBConstruct 1–374; UniProt 2–375

Methylated-DNA--protein-cysteine methyltransferase,Protein diaphanous homolog 1

Mus musculus

UniProt O08808

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 552–584 Chain E; UniProt 721–1255 Chain F; UniProt 552–584 Chain F; UniProt 721–1255 Not recorded Actin, cytoplasmic 1, N-terminally processed × 3 (P60709) ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;3 seconds, force 0. Resolution 3.49 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.

12 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DIAP1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 210–242; UniProt 552–584 Author chain E; PDBConstruct 243–777; UniProt 721–1255 Author chain F; PDBConstruct 210–242; UniProt 552–584 Author chain F; PDBConstruct 243–777; UniProt 721–1255

Methylated-DNA--protein-cysteine methyltransferase,Protein diaphanous homolog 1

Mus musculus

UniProt P16455

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–182 Chain F; UniProt 1–182 Not recorded Actin, cytoplasmic 1, N-terminally processed × 3 (P60709) ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;3 seconds, force 0. Resolution 3.49 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.

21 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MGMT_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 15–196; UniProt 1–182 Author chain F; PDBConstruct 15–196; UniProt 1–182

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 8ru2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ru2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ru2
Deposition date deposition_date2024-01-29
Structure title titleStructure of the F-actin barbed end bound by formin mDia1
Keywords keywordsactin, formin, Cdc12, profilin, actin assembly, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.49
Radius of gyration Rg (electron density) rg_electron44.21
Forward intensity I(0) i0656270000.00
Molecular weight molecular_weight210630.0 kDa
Excluded volume excluded_volume263570 ų
Envelope volume envelope_volume376910 ų
Hydration-shell volume shell_volume71364 ų
Envelope diameter envelope_diameter162.9
Shell Rg shell_rg48.83
Envelope Rg envelope_rg43.67
Shape Rg shape_rg44.23
Total Rg total_rg44.33
Total atoms total_atoms14773
Residues n_residues1846
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 dmax148.5
Rg (real space) rg_real44.37
Rg uncertainty (real space) rg_real_error1.53
I(0) (real space) i0_real6.5630e+08
I(0) uncertainty (real space) i0_real_error1.3020e+07
Rg (reciprocal space) rg_reciprocal44.49
I(0) (reciprocal space) i0_reciprocal656400000.0000
Solution quality estimate total_estimate0.8908
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.2
Skewness Skewness skewness0.209
Kurtosis Kurtosis kurtosis-0.422
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha50980000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.926

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)