6znm

The pointed end complex of dynactin bound to BICDR1

Method: ELECTRON MICROSCOPY Dmax: 208.9 Å Quality: GOOD

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

ARP1 actin related protein 1 homolog A

OrganismNot specified

UniProt F2Z5G5

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 1–376 Chain I; UniProt 1–376 Not recorded Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Dynactin subunit 2 × 1 (A0A5G2QD80) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICDR1 × 2 (A0JNT9) Dynactin subunit 4 × 1 (A0A4X1TB62) ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F2Z5G5_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain G; PDBConstruct 1–376; UniProt 1–376 Author chain I; PDBConstruct 1–376; UniProt 1–376

Actin, cytoplasmic 1

OrganismNot specified

UniProt Q6QAQ1

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain H; UniProt 1–375 Not recorded ARP1 actin related protein 1 homolog A × 2 (F2Z5G5) Arp11 × 1 (I3LHK5) Dynactin subunit 2 × 1 (A0A5G2QD80) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICDR1 × 2 (A0JNT9) Dynactin subunit 4 × 1 (A0A4X1TB62) ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

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

View Construct and Data Evidence
UniProt name ACTB_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–375; UniProt 1–375

Arp11

OrganismNot specified

UniProt I3LHK5

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain J; UniProt 1–417 Not recorded ARP1 actin related protein 1 homolog A × 2 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Dynactin subunit 2 × 1 (A0A5G2QD80) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICDR1 × 2 (A0JNT9) Dynactin subunit 4 × 1 (A0A4X1TB62) ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name I3LHK5_PIG
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–417; UniProt 1–417

Dynactin subunit 2

OrganismNot specified

UniProt A0A5G2QD80

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain M; UniProt 1–405 Not recorded ARP1 actin related protein 1 homolog A × 2 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICDR1 × 2 (A0JNT9) Dynactin subunit 4 × 1 (A0A4X1TB62) ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A5G2QD80_PIG
Isoform
PDB entities 4
Chains and sequence ranges Author chain M; PDBConstruct 1–405; UniProt 1–405

Dynactin 6

OrganismNot specified

UniProt D0G6S1

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain U; UniProt 1–190 Not recorded ARP1 actin related protein 1 homolog A × 2 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Dynactin subunit 2 × 1 (A0A5G2QD80) Dynactin subunit 5 × 1 (A0A286ZK88) BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICDR1 × 2 (A0JNT9) Dynactin subunit 4 × 1 (A0A4X1TB62) ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

20 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D0G6S1_PIG
Isoform
PDB entities 5
Chains and sequence ranges Author chain U; PDBConstruct 1–190; UniProt 1–190

Dynactin subunit 5

OrganismNot specified

UniProt A0A286ZK88

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain V; UniProt 1–182 Not recorded ARP1 actin related protein 1 homolog A × 2 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Dynactin subunit 2 × 1 (A0A5G2QD80) Dynactin 6 × 1 (D0G6S1) BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICDR1 × 2 (A0JNT9) Dynactin subunit 4 × 1 (A0A4X1TB62) ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

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

View Construct and Data Evidence
UniProt name A0A286ZK88_PIG
Isoform
PDB entities 6
Chains and sequence ranges Author chain V; PDBConstruct 1–182; UniProt 1–182

BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICDR1

Mus musculus

UniProt A0JNT9

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain X; UniProt 1–325 Chain x; UniProt 1–325 Not recorded ARP1 actin related protein 1 homolog A × 2 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Dynactin subunit 2 × 1 (A0A5G2QD80) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BICL1_MOUSE
Isoform
PDB entities 7
Chains and sequence ranges Author chain X; PDBConstruct 1–325; UniProt 1–325 Author chain x; PDBConstruct 1–325; UniProt 1–325

Dynactin subunit 4

OrganismNot specified

UniProt A0A4X1TB62

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain Y; UniProt 1–467 Not recorded ARP1 actin related protein 1 homolog A × 2 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Dynactin subunit 2 × 1 (A0A5G2QD80) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICDR1 × 2 (A0JNT9) ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A4X1TB62_PIG
Isoform
PDB entities 8
Chains and sequence ranges Author chain Y; PDBConstruct 1–467; UniProt 1–467

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 6znm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6znm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6znm
Deposition date deposition_date2020-07-06
Structure title titleThe pointed end complex of dynactin bound to BICDR1
Keywords keywordsDynactin, Complex, Scaffold, 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_guinier53.71
Radius of gyration Rg (electron density) rg_electron54.00
Forward intensity I(0) i01103140000.00
Molecular weight molecular_weight273630.0 kDa
Excluded volume excluded_volume341310 ų
Envelope volume envelope_volume502220 ų
Hydration-shell volume shell_volume81669 ų
Envelope diameter envelope_diameter229.1
Shell Rg shell_rg52.42
Envelope Rg envelope_rg54.27
Shape Rg shape_rg54.07
Total Rg total_rg53.71
Total atoms total_atoms19253
Residues n_residues2601
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 dmax208.9
Rg (real space) rg_real54.22
Rg uncertainty (real space) rg_real_error3.04
I(0) (real space) i0_real1.1030e+09
I(0) uncertainty (real space) i0_real_error2.8790e+07
Rg (reciprocal space) rg_reciprocal53.28
I(0) (reciprocal space) i0_reciprocal1102000000.0000
Solution quality estimate total_estimate0.7838
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.4
Skewness Skewness skewness0.674
Kurtosis Kurtosis kurtosis0.118
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha117300000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.493; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.810; Smooth: 0.897

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)