6f3a

Cryo-EM structure of a single dynein tail domain bound to dynactin and BICD2N

Method: ELECTRON MICROSCOPY Dmax: 268.8 Å Quality: EXCELLENT

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain A; UniProt 1–376 Chain B; UniProt 1–376 Chain C; UniProt 1–376 Chain D; UniProt 1–376 Chain E; UniProt 1–376 Chain F; UniProt 1–376 Chain G; UniProt 1–376 Chain I; UniProt 1–376 Not recorded Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin related protein 10 homolog × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin capping protein beta subunit × 1 (A9XFX6) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Dynactin subunit 2 × 1 (F1SKF9) Dynactin subunit 2 × 3 (F1SKF9) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 A; PDBConstruct 1–376; UniProt 1–376 Author chain B; PDBConstruct 1–376; UniProt 1–376 Author chain C; PDBConstruct 1–376; UniProt 1–376 Author chain D; PDBConstruct 1–376; UniProt 1–376 Author chain E; PDBConstruct 1–376; UniProt 1–376 Author chain F; PDBConstruct 1–376; UniProt 1–376 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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain H; UniProt 1–375 Not recorded ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin related protein 10 homolog × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin capping protein beta subunit × 1 (A9XFX6) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Dynactin subunit 2 × 1 (F1SKF9) Dynactin subunit 2 × 3 (F1SKF9) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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

Actin related protein 10 homolog

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain J; UniProt 1–390 Not recorded ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin capping protein beta subunit × 1 (A9XFX6) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Dynactin subunit 2 × 1 (F1SKF9) Dynactin subunit 2 × 3 (F1SKF9) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 1–390; UniProt 1–390

Capping protein (Actin filament) muscle Z-line, alpha 1

OrganismNot specified

UniProt A0PFK5

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain K; UniProt 1–286 Not recorded ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin related protein 10 homolog × 1 (I3LHK5) F-actin capping protein beta subunit × 1 (A9XFX6) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Dynactin subunit 2 × 1 (F1SKF9) Dynactin subunit 2 × 3 (F1SKF9) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 A0PFK5_PIG
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 1–286; UniProt 1–286

F-actin capping protein beta subunit

OrganismNot specified

UniProt A9XFX6

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain L; UniProt 1–272 Not recorded ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin related protein 10 homolog × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Dynactin subunit 2 × 1 (F1SKF9) Dynactin subunit 2 × 3 (F1SKF9) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A9XFX6_PIG
Isoform
PDB entities 5
Chains and sequence ranges Author chain L; PDBConstruct 1–272; UniProt 1–272

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain U; UniProt 1–190 Not recorded ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin related protein 10 homolog × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin capping protein beta subunit × 1 (A9XFX6) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Dynactin subunit 2 × 1 (F1SKF9) Dynactin subunit 2 × 3 (F1SKF9) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 10
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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain V; UniProt 1–182 Not recorded ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin related protein 10 homolog × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin capping protein beta subunit × 1 (A9XFX6) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin 6 × 1 (D0G6S1) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Dynactin subunit 2 × 1 (F1SKF9) Dynactin subunit 2 × 3 (F1SKF9) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 11
Chains and sequence ranges Author chain V; PDBConstruct 1–182; UniProt 1–182

Dynactin subunit 2

OrganismNot specified

UniProt F1SKF9

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain a; UniProt 1–68 Chain b; UniProt 1–89 Chain c; UniProt 1–89 Chain d; UniProt 1–89 Not recorded ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin related protein 10 homolog × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin capping protein beta subunit × 1 (A9XFX6) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F1SKF9_PIG
Isoform
PDB entities 14, 15
Chains and sequence ranges Author chain a; PDBConstruct 1–68; UniProt 1–68 Author chain b; PDBConstruct 1–89; UniProt 1–89 Author chain c; PDBConstruct 1–89; UniProt 1–89 Author chain d; PDBConstruct 1–89; UniProt 1–89

Cytoplasmic dynein 1 heavy chain 1

Homo sapiens

UniProt Q14204

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain e; UniProt 1–1455 Chain f; UniProt 1–1455 Not recorded ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin related protein 10 homolog × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin capping protein beta subunit × 1 (A9XFX6) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Dynactin subunit 2 × 1 (F1SKF9) Dynactin subunit 2 × 3 (F1SKF9) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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.

96 other PDB entries and 97 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DYHC1_HUMAN
Isoform
PDB entities 16
Chains and sequence ranges Author chain e; PDBConstruct 1–1455; UniProt 1–1455 Author chain f; PDBConstruct 1–1455; UniProt 1–1455

Cytoplasmic dynein 1 intermediate chain 2

Homo sapiens

UniProt Q13409

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain g; UniProt 1–612 Chain h; UniProt 1–612 Not recorded ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin related protein 10 homolog × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin capping protein beta subunit × 1 (A9XFX6) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Dynactin subunit 2 × 1 (F1SKF9) Dynactin subunit 2 × 3 (F1SKF9) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DC1I2_HUMAN
Isoform Q13409-3
PDB entities 17
Chains and sequence ranges Author chain g; PDBConstruct 1–612; UniProt 1–612 Author chain h; PDBConstruct 1–612; UniProt 1–612

Cytoplasmic dynein 1 light intermediate chain 2

Homo sapiens

UniProt O43237

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain j; UniProt 1–492 Not recorded ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin related protein 10 homolog × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin capping protein beta subunit × 1 (A9XFX6) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Dynactin subunit 2 × 1 (F1SKF9) Dynactin subunit 2 × 3 (F1SKF9) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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.

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DC1L2_HUMAN
Isoform
PDB entities 18
Chains and sequence ranges Author chain j; PDBConstruct 1–492; UniProt 1–492

Dynein light chain roadblock-type 1

Homo sapiens

UniProt Q9NP97

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain k; UniProt 1–96 Chain l; UniProt 1–96 Not recorded ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin related protein 10 homolog × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin capping protein beta subunit × 1 (A9XFX6) Dynactin Subunit 2 × 1 Dynactin Subunit 2 × 1 Dynactin Subunit 3 × 2 Dynactin Subunit 2 × 2 Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin Subunit 4 × 1 Dynactin Subunit 1 × 1 Dynactin subunit 2 × 1 (F1SKF9) Dynactin subunit 2 × 3 (F1SKF9) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) Dynactin Subunit 1 × 1 BICD2N × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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.

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

View Construct and Data Evidence
UniProt name DLRB1_HUMAN
Isoform
PDB entities 19
Chains and sequence ranges Author chain k; PDBConstruct 1–96; UniProt 1–96 Author chain l; PDBConstruct 1–96; UniProt 1–96

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 6f3a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6f3a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6f3a
Deposition date deposition_date2017-11-28
Structure title titleCryo-EM structure of a single dynein tail domain bound to dynactin and BICD2N
Keywords keywordsTDB, dynein/dynactin/BICD2, complex, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier97.74
Radius of gyration Rg (electron density) rg_electron99.40
Forward intensity I(0) i09746190000.00
Molecular weight molecular_weight684470.0 kDa
Excluded volume excluded_volume787700 ų
Envelope volume envelope_volume2064400 ų
Hydration-shell volume shell_volume192270 ų
Envelope diameter envelope_diameter389.6
Shell Rg shell_rg80.55
Envelope Rg envelope_rg95.81
Shape Rg shape_rg99.42
Total Rg total_rg99.14
Total atoms total_atoms48864
Residues n_residues9811
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 dmax268.8
Rg (real space) rg_real91.86
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real9.3040e+09
I(0) uncertainty (real space) i0_real_error2.1210e+08
Rg (reciprocal space) rg_reciprocal92.99
I(0) (reciprocal space) i0_reciprocal9595000000.0000
Solution quality estimate total_estimate0.9160
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary117.6
Skewness Skewness skewness0.341
Kurtosis Kurtosis kurtosis-0.456
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.7338
Highest regularization parameter α highest_alpha483200000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.026; Oscil: 0.996; Stabil: 0.978; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.008

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (23)

8. Citations (1)

9. Files and Curves (10)