6d8c

Cryo-EM structure of FLNaABD E254K bound to phalloidin-stabilized F-actin

Method: ELECTRON MICROSCOPY Dmax: 179.6 Å Quality: GOOD

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

Filamin-A

Homo sapiens

UniProt P21333

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain A; UniProt 1–278 Chain B; UniProt 1–278 Chain C; UniProt 1–278 Chain D; UniProt 1–278 Chain E; UniProt 1–278 Fragment:UNP residues 1-278 Mutation:E254K Actin, alpha skeletal muscle × 5 (P68139) Phalloidin × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.54 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.

25 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLNA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 29–306; UniProt 1–278 Author chain B; PDBConstruct 29–306; UniProt 1–278 Author chain C; PDBConstruct 29–306; UniProt 1–278 Author chain D; PDBConstruct 29–306; UniProt 1–278 Author chain E; PDBConstruct 29–306; UniProt 1–278

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68139

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 × 13 PDB declaration: tridecameric(13) Consistent with protein copy count Chain H; UniProt 3–377 Chain J; UniProt 3–377 Chain K; UniProt 3–377 Chain L; UniProt 3–377 Chain M; UniProt 3–377 Not recorded Filamin-A × 5 (P21333) Phalloidin × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.54 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.

57 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_CHICK
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–375; UniProt 3–377 Author chain J; PDBConstruct 1–375; UniProt 3–377 Author chain K; PDBConstruct 1–375; UniProt 3–377 Author chain L; PDBConstruct 1–375; UniProt 3–377 Author chain M; PDBConstruct 1–375; UniProt 3–377

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 6d8c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6d8c
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6d8c
Deposition date deposition_date2018-04-26
Structure title titleCryo-EM structure of FLNaABD E254K bound to phalloidin-stabilized F-actin
Keywords keywordsActin-binding domain, Actin crosslinker, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.36
Radius of gyration Rg (electron density) rg_electron50.62
Forward intensity I(0) i01140630000.00
Molecular weight molecular_weight280450.0 kDa
Excluded volume excluded_volume351030 ų
Envelope volume envelope_volume471080 ų
Hydration-shell volume shell_volume79952 ų
Envelope diameter envelope_diameter197.3
Shell Rg shell_rg51.45
Envelope Rg envelope_rg50.65
Shape Rg shape_rg50.62
Total Rg total_rg50.64
Total atoms total_atoms39316
Residues n_residues2467
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 dmax179.6
Rg (real space) rg_real50.59
Rg uncertainty (real space) rg_real_error2.06
I(0) (real space) i0_real1.1410e+09
I(0) uncertainty (real space) i0_real_error2.3970e+07
Rg (reciprocal space) rg_reciprocal50.17
I(0) (reciprocal space) i0_reciprocal1140000000.0000
Solution quality estimate total_estimate0.8372
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.1
Skewness Skewness skewness0.530
Kurtosis Kurtosis kurtosis-0.148
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha105000000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.732; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.887; Smooth: 0.796

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 25 domains

CATH v4.4 (25 domains)

Domain ID domain_id6d8cA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily10 — Calponin-like domain
Domain ID domain_id6d8cB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily10 — Calponin-like domain
Domain ID domain_id6d8cC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily10 — Calponin-like domain
Domain ID domain_id6d8cD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily10 — Calponin-like domain
Domain ID domain_id6d8cE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily10 — Calponin-like domain
Domain ID domain_id6d8cH01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id6d8cH02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology36 — Actin; Chain A, domain 2
Homologous superfamily homologous superfamily70 — Actin; Chain A, domain 2
Domain ID domain_id6d8cH03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id6d8cH04
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id6d8cJ01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id6d8cJ02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology36 — Actin; Chain A, domain 2
Homologous superfamily homologous superfamily70 — Actin; Chain A, domain 2
Domain ID domain_id6d8cJ03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id6d8cJ04
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id6d8cK01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id6d8cK02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology36 — Actin; Chain A, domain 2
Homologous superfamily homologous superfamily70 — Actin; Chain A, domain 2
Domain ID domain_id6d8cK03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id6d8cK04
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id6d8cL01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id6d8cL02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology36 — Actin; Chain A, domain 2
Homologous superfamily homologous superfamily70 — Actin; Chain A, domain 2
Domain ID domain_id6d8cL03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id6d8cL04
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id6d8cM01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id6d8cM02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology36 — Actin; Chain A, domain 2
Homologous superfamily homologous superfamily70 — Actin; Chain A, domain 2
Domain ID domain_id6d8cM03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id6d8cM04
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4

8. Citations (1)

9. Files and Curves (10)