9yng

Dynactin and dynein-1 tail region of dynein-dynactin complex on microtubule in the presence of LIS1

Method: ELECTRON MICROSCOPY Dmax: 293.7 Å Quality: EXCELLENT

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

Alpha-centractin

Sus scrofa

UniProt A0A8D1PMN0

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 × 31 PDB declaration: 31-meric(31) 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 × 1 (I3LHK5) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 1 × 2 (A0A287B8J2) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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 A0A8D1PMN0_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

Sus scrofa

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain H; UniProt 1–375 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin-related protein 10 × 1 (I3LHK5) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 1 × 2 (A0A287B8J2) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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

Sus scrofa

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain J; UniProt 1–417 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin, cytoplasmic 1 × 1 (Q6QAQ1) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 1 × 2 (A0A287B8J2) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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 ARP10_PIG
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–417; UniProt 1–417

F-actin-capping protein subunit alpha-1

Sus scrofa

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain K; UniProt 1–286 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin-related protein 10 × 1 (I3LHK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 1 × 2 (A0A287B8J2) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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 CAZA1_PIG
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 1–286; UniProt 1–286

F-actin-capping protein subunit beta

Sus scrofa

UniProt A0PFK7

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain L; UniProt 1–272 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin-related protein 10 × 1 (I3LHK5) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 1 × 2 (A0A287B8J2) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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

Dynactin subunit 2

Sus scrofa

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain M; UniProt 1–405 Chain N; UniProt 1–405 Chain P; UniProt 1–405 Chain Q; UniProt 1–405 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin-related protein 10 × 1 (I3LHK5) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 1 × 2 (A0A287B8J2) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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 DCTN2_PIG
Isoform
PDB entities 6
Chains and sequence ranges Author chain M; PDBConstruct 1–405; UniProt 1–405 Author chain N; PDBConstruct 1–405; UniProt 1–405 Author chain P; PDBConstruct 1–405; UniProt 1–405 Author chain Q; PDBConstruct 1–405; UniProt 1–405

Dynactin subunit 3

Sus scrofa

UniProt F1SEC0

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain O; UniProt 1–186 Chain R; UniProt 1–186 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin-related protein 10 × 1 (I3LHK5) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 1 × 2 (A0A287B8J2) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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 DCTN3_PIG
Isoform
PDB entities 7
Chains and sequence ranges Author chain O; PDBConstruct 1–186; UniProt 1–186 Author chain R; PDBConstruct 1–186; UniProt 1–186

Dynactin subunit 6

Sus scrofa

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain U; UniProt 1–190 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin-related protein 10 × 1 (I3LHK5) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 1 × 2 (A0A287B8J2) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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 DCTN6_PIG
Isoform
PDB entities 8
Chains and sequence ranges Author chain U; PDBConstruct 1–190; UniProt 1–190

Dynactin subunit 5

Sus scrofa

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain V; UniProt 1–182 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin-related protein 10 × 1 (I3LHK5) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 1 × 2 (A0A287B8J2) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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 DCTN5_PIG
Isoform
PDB entities 9
Chains and sequence ranges Author chain V; PDBConstruct 1–182; UniProt 1–182

Dynactin subunit 1

Sus scrofa

UniProt A0A287B8J2

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain W; UniProt 1–1281 Chain Z; UniProt 1–1281 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin-related protein 10 × 1 (I3LHK5) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCTN1_PIG
Isoform
PDB entities 10
Chains and sequence ranges Author chain W; PDBConstruct 1–1281; UniProt 1–1281 Author chain Z; PDBConstruct 1–1281; UniProt 1–1281

Dynactin subunit 4

Sus scrofa

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain Y; UniProt 1–467 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin-related protein 10 × 1 (I3LHK5) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 1 × 2 (A0A287B8J2) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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 DCTN4_PIG
Isoform
PDB entities 11
Chains and sequence ranges Author chain Y; PDBConstruct 1–467; UniProt 1–467

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain e; UniProt 1–4646 Chain f; UniProt 1–4646 Chain m; UniProt 1–4646 Chain n; UniProt 1–4646 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin-related protein 10 × 1 (I3LHK5) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 1 × 2 (A0A287B8J2) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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 12
Chains and sequence ranges Author chain e; PDBConstruct 1–4646; UniProt 1–4646 Author chain f; PDBConstruct 1–4646; UniProt 1–4646 Author chain m; PDBConstruct 1–4646; UniProt 1–4646 Author chain n; PDBConstruct 1–4646; UniProt 1–4646

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 × 31 PDB declaration: 31-meric(31) Consistent with protein copy count Chain g; UniProt 1–638 Chain h; UniProt 1–638 Chain o; UniProt 1–638 Chain p; UniProt 1–638 Not recorded Alpha-centractin × 8 (A0A8D1PMN0) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Actin-related protein 10 × 1 (I3LHK5) F-actin-capping protein subunit alpha-1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 4 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 1 × 2 (A0A287B8J2) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.07 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
PDB entities 13
Chains and sequence ranges Author chain g; PDBConstruct 1–638; UniProt 1–638 Author chain h; PDBConstruct 1–638; UniProt 1–638 Author chain o; PDBConstruct 1–638; UniProt 1–638 Author chain p; PDBConstruct 1–638; UniProt 1–638

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 9yng

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9yng
Deposition date deposition_date2025-10-10
Structure title titleDynactin and dynein-1 tail region of dynein-dynactin complex on microtubule in the presence of LIS1
Keywords keywordsDynein-1, Dynactin, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron109.10
Forward intensity I(0) i020421700000.00
Molecular weight molecular_weight1181300.0 kDa
Excluded volume excluded_volume1461900 ų
Envelope volume envelope_volume2793400 ų
Hydration-shell volume shell_volume235900 ų
Envelope diameter envelope_diameter453.8
Shell Rg shell_rg86.96
Envelope Rg envelope_rg107.60
Shape Rg shape_rg109.10
Total Rg total_rg108.90
Total atoms total_atoms83396
Residues n_residues11583
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 dmax293.7
Rg (real space) rg_real100.10
Rg uncertainty (real space) rg_real_error1.46
I(0) (real space) i0_real1.9480e+10
I(0) uncertainty (real space) i0_real_error4.7770e+08
Rg (reciprocal space) rg_reciprocal99.08
I(0) (reciprocal space) i0_reciprocal19870000000.0000
Solution quality estimate total_estimate0.9179
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary104.9
Skewness Skewness skewness0.373
Kurtosis Kurtosis kurtosis-0.474
Angular range angular_range— – 0.0700 −1
Current regularization parameter α current_alpha0.6566
Highest regularization parameter α highest_alpha551700000.0000
Real-space data points n_real_points15
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.024; Oscil: 0.995; Stabil: 0.983; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.007

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (1)

9. Files and Curves (10)