9hhl

Structure of Dynein-Dynactin-NuMA-LIS1

Method: ELECTRON MICROSCOPY Dmax: 309.0 Å Quality: EXCELLENT

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

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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain g; UniProt 1–612 Chain h; UniProt 1–612 Chain o; UniProt 1–612 Chain p; UniProt 1–612 Not recorded Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 1
Chains and sequence ranges Author chain g; PDBConstruct 1–612; UniProt 1–612 Author chain h; PDBConstruct 1–612; UniProt 1–612 Author chain o; PDBConstruct 1–612; UniProt 1–612 Author chain p; PDBConstruct 1–612; UniProt 1–612

Nuclear mitotic apparatus protein 1,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 × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain 1; UniProt 1–182 Chain 2; UniProt 1–182 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 1; PDBConstruct 708–889; UniProt 1–182 Author chain 2; PDBConstruct 708–889; UniProt 1–182

Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase

Homo sapiens

UniProt Q14980

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 × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain 1; UniProt 1–705 Chain 2; UniProt 1–705 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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.

4 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUMA1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain 1; PDBConstruct 1–705; UniProt 1–705 Author chain 2; PDBConstruct 1–705; UniProt 1–705

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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) 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 Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 3
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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain H; UniProt 1–375 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 4
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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain J; UniProt 1–417 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) 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 subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 5
Chains and sequence ranges Author chain J; PDBConstruct 1–417; UniProt 1–417

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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain K; UniProt 1–286 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 6
Chains and sequence ranges Author chain K; PDBConstruct 1–286; UniProt 1–286

F-actin-capping protein subunit beta

OrganismNot specified

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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain L; UniProt 1–272 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 7
Chains and sequence ranges Author chain L; PDBConstruct 1–272; UniProt 1–272

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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) 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 Chain V; UniProt 1–405 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 8
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 Author chain V; PDBConstruct 1–405; UniProt 1–405

Dynactin subunit 3

OrganismNot specified

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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain O; UniProt 1–186 Chain R; UniProt 1–186 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 F1SEC0_PIG
Isoform
PDB entities 9
Chains and sequence ranges Author chain O; PDBConstruct 1–186; UniProt 1–186 Author chain R; PDBConstruct 1–186; UniProt 1–186

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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain U; UniProt 1–190 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain W; UniProt 1–182 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 W; PDBConstruct 1–182; UniProt 1–182

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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain Y; UniProt 1–467 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 12
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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) 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 Mutation:R1567E, K1610E Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 13
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 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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain j; UniProt 1–492 Chain q; UniProt 1–492 Chain u; UniProt 1–492 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Dynein light chain roadblock-type 1 × 4 (Q9NP97) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 14
Chains and sequence ranges Author chain j; PDBConstruct 1–492; UniProt 1–492 Author chain q; PDBConstruct 1–492; UniProt 1–492 Author chain u; 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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain s; UniProt 1–96 Chain t; UniProt 1–96 Chain w; UniProt 1–96 Chain z; UniProt 1–96 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 15
Chains and sequence ranges Author chain s; PDBConstruct 1–96; UniProt 1–96 Author chain t; PDBConstruct 1–96; UniProt 1–96 Author chain w; PDBConstruct 1–96; UniProt 1–96 Author chain z; PDBConstruct 1–96; UniProt 1–96

Dynactin subunit 1

OrganismNot specified

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 Insufficient information Heteromer Protein × 41 PDB declaration: 41-meric(41) Consistent with protein copy count Chain S; UniProt 1–1281 Chain T; UniProt 1–1281 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 4 (Q13409) Nuclear mitotic apparatus protein 1,Methylated-DNA--protein-cysteine methyltransferase × 2 (Q14980,P16455) ARP1 actin related protein 1 homolog A × 8 (F2Z5G5) Actin, cytoplasmic 1 × 1 (Q6QAQ1) Arp11 × 1 (I3LHK5) Capping protein (Actin filament) muscle Z-line, alpha 1 × 1 (A0PFK5) F-actin-capping protein subunit beta × 1 (A0PFK7) Dynactin subunit 2 × 5 (A0A5G2QD80) Dynactin subunit 3 × 2 (F1SEC0) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) Cytoplasmic dynein 1 heavy chain 1 × 4 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 3 (O43237) Dynein light chain roadblock-type 1 × 4 (Q9NP97) ADP ADENOSINE-5'-DIPHOSPHATE × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.53 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 16
Chains and sequence ranges Author chain S; PDBConstruct 1–1281; UniProt 1–1281 Author chain T; PDBConstruct 1–1281; UniProt 1–1281

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 9hhl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9hhl
Deposition date deposition_date2024-11-21
Structure title titleStructure of Dynein-Dynactin-NuMA-LIS1
Keywords keywordsmotor protein, transport; 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_electron114.80
Forward intensity I(0) i016982700000.00
Molecular weight molecular_weight904390.0 kDa
Excluded volume excluded_volume1039400 ų
Envelope volume envelope_volume2961800 ų
Hydration-shell volume shell_volume240470 ų
Envelope diameter envelope_diameter459.7
Shell Rg shell_rg90.92
Envelope Rg envelope_rg110.40
Shape Rg shape_rg114.80
Total Rg total_rg114.60
Total atoms total_atoms64583
Residues n_residues12994
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 dmax309.0
Rg (real space) rg_real105.20
Rg uncertainty (real space) rg_real_error1.57
I(0) (real space) i0_real1.6230e+10
I(0) uncertainty (real space) i0_real_error3.5880e+08
Rg (reciprocal space) rg_reciprocal103.90
I(0) (reciprocal space) i0_reciprocal16470000000.0000
Solution quality estimate total_estimate0.9187
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary118.9
Skewness Skewness skewness0.342
Kurtosis Kurtosis kurtosis-0.492
Angular range angular_range— – 0.0650 −1
Current regularization parameter α current_alpha0.5092
Highest regularization parameter α highest_alpha736400000.0000
Real-space data points n_real_points14
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.013; Oscil: 0.997; Stabil: 0.987; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (19)

8. Citations (1)

9. Files and Curves (10)