9qfk

Cryo-EM structure of the Coronin-1B-decorated actin filament bound by one Cofilin-1 molecule (crosslinked)

Method: ELECTRON MICROSCOPY Dmax: 214.8 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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain A; UniProt 2–375 Chain B; UniProt 2–375 Chain C; UniProt 2–375 Chain D; UniProt 2–375 Chain E; UniProt 2–375 Chain F; UniProt 2–375 Chain G; UniProt 2–375 Mutation:C272A Non-standard monomer:Yes (specific site not provided by mmCIF) Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase × 6 (Q9BR76,P16455) Cofilin-1 × 1 (P23528) ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1;1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.02% Tween20). cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.99 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 A; PDBConstruct 1–374; UniProt 2–375 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 Author chain E; PDBConstruct 1–374; UniProt 2–375 Author chain F; PDBConstruct 1–374; UniProt 2–375 Author chain G; PDBConstruct 1–374; UniProt 2–375

Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase

Homo sapiens

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain H; UniProt 1–182 Chain I; UniProt 1–182 Chain K; UniProt 1–182 Chain L; UniProt 1–182 Chain M; UniProt 1–182 Chain N; UniProt 1–182 Not recorded Actin, cytoplasmic 1, N-terminally processed × 7 (P60709) Cofilin-1 × 1 (P23528) ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1;1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.02% Tween20). cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.99 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 H; PDBConstruct 507–688; UniProt 1–182 Author chain I; PDBConstruct 507–688; UniProt 1–182 Author chain K; PDBConstruct 507–688; UniProt 1–182 Author chain L; PDBConstruct 507–688; UniProt 1–182 Author chain M; PDBConstruct 507–688; UniProt 1–182 Author chain N; PDBConstruct 507–688; UniProt 1–182

Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase

Homo sapiens

UniProt Q9BR76

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain H; UniProt 1–489 Chain I; UniProt 1–489 Chain K; UniProt 1–489 Chain L; UniProt 1–489 Chain M; UniProt 1–489 Chain N; UniProt 1–489 Not recorded Actin, cytoplasmic 1, N-terminally processed × 7 (P60709) Cofilin-1 × 1 (P23528) ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1;1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.02% Tween20). cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.99 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COR1B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 6–494; UniProt 1–489 Author chain I; PDBConstruct 6–494; UniProt 1–489 Author chain K; PDBConstruct 6–494; UniProt 1–489 Author chain L; PDBConstruct 6–494; UniProt 1–489 Author chain M; PDBConstruct 6–494; UniProt 1–489 Author chain N; PDBConstruct 6–494; UniProt 1–489

Cofilin-1

Homo sapiens

UniProt P23528

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain J; UniProt 1–166 Not recorded Actin, cytoplasmic 1, N-terminally processed × 7 (P60709) Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase × 6 (Q9BR76,P16455) ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1;1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.02% Tween20). cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.99 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.

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

View Construct and Data Evidence
UniProt name COF1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–166; UniProt 1–166

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 9qfk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qfk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9qfk
Deposition date deposition_date2025-03-11
Structure title titleCryo-EM structure of the Coronin-1B-decorated actin filament bound by one Cofilin-1 molecule (crosslinked)
Keywords keywordsactin, coronin, cofilin, filament, cytoskeleton, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.19
Radius of gyration Rg (electron density) rg_electron67.57
Forward intensity I(0) i04588230000.00
Molecular weight molecular_weight569880.0 kDa
Excluded volume excluded_volume711970 ų
Envelope volume envelope_volume994530 ų
Hydration-shell volume shell_volume127040 ų
Envelope diameter envelope_diameter252.9
Shell Rg shell_rg62.96
Envelope Rg envelope_rg67.00
Shape Rg shape_rg67.60
Total Rg total_rg67.39
Total atoms total_atoms40017
Residues n_residues5073
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 dmax214.8
Rg (real space) rg_real67.37
Rg uncertainty (real space) rg_real_error1.88
I(0) (real space) i0_real4.5870e+09
I(0) uncertainty (real space) i0_real_error1.0310e+08
Rg (reciprocal space) rg_reciprocal66.23
I(0) (reciprocal space) i0_reciprocal4578000000.0000
Solution quality estimate total_estimate0.8271
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.4
Skewness Skewness skewness0.490
Kurtosis Kurtosis kurtosis-0.354
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0007
Highest regularization parameter α highest_alpha305600000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.904; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.053

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)