9qey

Cryo-EM structure of the actin filament bound by a single Coronin-1B molecule.

Method: ELECTRON MICROSCOPY Dmax: 173.1 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 × 6 PDB declaration: hexameric(6) 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 Mutation:C272A Non-standard monomer:Yes (specific site not provided by mmCIF) Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase × 1 (Q9BR76,P16455) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 PO4 PHOSPHATE ION × 5 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, 0.01% Tween20). cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.74 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

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain H; UniProt 1–182 Not recorded Actin, cytoplasmic 1, N-terminally processed × 5 (P60709) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 PO4 PHOSPHATE ION × 5 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, 0.01% Tween20). cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.74 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

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain H; UniProt 1–489 Not recorded Actin, cytoplasmic 1, N-terminally processed × 5 (P60709) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 PO4 PHOSPHATE ION × 5 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, 0.01% Tween20). cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.74 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

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 9qey

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9qey
Deposition date deposition_date2025-03-11
Structure title titleCryo-EM structure of the actin filament bound by a single Coronin-1B molecule.
Keywords keywordsactin, coronin, 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_guinier46.89
Radius of gyration Rg (electron density) rg_electron47.10
Forward intensity I(0) i0944303000.00
Molecular weight molecular_weight251440.0 kDa
Excluded volume excluded_volume313250 ų
Envelope volume envelope_volume408590 ų
Hydration-shell volume shell_volume74723 ų
Envelope diameter envelope_diameter185.4
Shell Rg shell_rg49.36
Envelope Rg envelope_rg46.64
Shape Rg shape_rg47.11
Total Rg total_rg47.14
Total atoms total_atoms17622
Residues n_residues2231
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 dmax173.1
Rg (real space) rg_real47.12
Rg uncertainty (real space) rg_real_error2.23
I(0) (real space) i0_real9.4430e+08
I(0) uncertainty (real space) i0_real_error1.9030e+07
Rg (reciprocal space) rg_reciprocal46.89
I(0) (reciprocal space) i0_reciprocal944000000.0000
Solution quality estimate total_estimate0.8453
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.9
Skewness Skewness skewness0.496
Kurtosis Kurtosis kurtosis-0.117
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha101200000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.686; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.948

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)