5adx

CryoEM structure of dynactin complex at 4.0 angstrom resolution

Method: ELECTRON MICROSCOPY

▼

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

ACTIN RELATED PROTEIN 1

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 27	ACTIN, CYTOPLASMIC 1 × 1 （Q6QAQ1） ACTIN RELATED PROTEIN 11 × 1 （I3LHK5） CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 （A0PFK5） F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 （D2JYW4） DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 3 × 2 DYNACTIN SUBUNIT 2 × 2 DYNACTIN 5 × 1 （D0G6S1） DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	F2Z5G5_PIG
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–370； UniProt 7–376 Author chain B； PDBConstruct 1–370； UniProt 7–376 Author chain C； PDBConstruct 1–370； UniProt 7–376 Author chain D； PDBConstruct 1–370； UniProt 7–376 Author chain E； PDBConstruct 1–370； UniProt 7–376 Author chain F； PDBConstruct 1–370； UniProt 7–376 Author chain G； PDBConstruct 1–370； UniProt 7–376 Author chain I； PDBConstruct 1–370； UniProt 7–376

ACTIN, CYTOPLASMIC 1

OrganismNot specified

UniProt Q6QAQ1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 27	ACTIN RELATED PROTEIN 1 × 8 （F2Z5G5） ACTIN RELATED PROTEIN 11 × 1 （I3LHK5） CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 （A0PFK5） F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 （D2JYW4） DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 3 × 2 DYNACTIN SUBUNIT 2 × 2 DYNACTIN 5 × 1 （D0G6S1） DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ACTB_PIG
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain H； PDBConstruct 1–370； UniProt 6–375

ACTIN RELATED PROTEIN 11

OrganismNot specified

UniProt I3LHK5

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 27	ACTIN RELATED PROTEIN 1 × 8 （F2Z5G5） ACTIN, CYTOPLASMIC 1 × 1 （Q6QAQ1） CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 （A0PFK5） F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 （D2JYW4） DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 3 × 2 DYNACTIN SUBUNIT 2 × 2 DYNACTIN 5 × 1 （D0G6S1） DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1	Consistent with protein count

Other States of the Same Protein in the Database

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

CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1

OrganismNot specified

UniProt A0PFK5

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 27	ACTIN RELATED PROTEIN 1 × 8 （F2Z5G5） ACTIN, CYTOPLASMIC 1 × 1 （Q6QAQ1） ACTIN RELATED PROTEIN 11 × 1 （I3LHK5） F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 （D2JYW4） DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 3 × 2 DYNACTIN SUBUNIT 2 × 2 DYNACTIN 5 × 1 （D0G6S1） DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0PFK5_PIG
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain K； PDBConstruct 1–275； UniProt 7–281

F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II

OrganismNot specified

UniProt D2JYW4

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 27	ACTIN RELATED PROTEIN 1 × 8 （F2Z5G5） ACTIN, CYTOPLASMIC 1 × 1 （Q6QAQ1） ACTIN RELATED PROTEIN 11 × 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 5 × 1 （D0G6S1） DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	D2JYW4_PIG
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain L； PDBConstruct 1–270； UniProt 2–271

DYNACTIN 5

OrganismNot specified

UniProt D0G6S1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 27	ACTIN RELATED PROTEIN 1 × 8 （F2Z5G5） ACTIN, CYTOPLASMIC 1 × 1 （Q6QAQ1） ACTIN RELATED PROTEIN 11 × 1 （I3LHK5） CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 （A0PFK5） F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 （D2JYW4） DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 3 × 2 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	D0G6S1_PIG
Isoform	—
PDB entities	10
Chains and sequence ranges	Author chain U； PDBConstruct 1–189； UniProt 1–190

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	5adx
Deposition date deposition_date	2015-08-24
Structure title title	CryoEM structure of dynactin complex at 4.0 angstrom resolution
Keywords keywords	STRUCTURAL PROTEIN, DYNEIN CO-FACTOR, ACTIN-LIKE FILAMENT, CELLULAR CARGO TRANSPORT; STRUCTURAL PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

5adx__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5adx__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5adx__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	98.41 Å
Rg (electron density)	99.99 Å
Total Rg	99.28 Å
Atom count	49392
Residues	7306
Excluded volume	858580 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5adx__assembly_1__model_1`	27-meric （27）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (17)

Entity 1 Entity 1 polymer

Description description	ACTIN RELATED PROTEIN 1
Molecular weight formula_weight	41959.9 kDa
Source method src_method	nat
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,I
Atom count atom_count	49392

IANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHVRVMAGALEGDIFIGPKAEEHRGLLSIRYPMEHGIVKDWNDMERIWQYVYSKEQLQTFSEEHPVLLTEAPLNPRKNRERAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRIDIAGRDVSRFLRLYLRKEGYDFHSSSEFEIVKAIKERACYLSINPQKDETLETEKAQYYLPDGSTIEIGPSRFRAPELLFRPDLIGEESEGIHEVLVFAIQKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGARSIHRKTF

Entity 2 Entity 2 polymer

Description description	ACTIN, CYTOPLASMIC 1
Molecular weight formula_weight	41193.0 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

Entity 3 Entity 3 polymer

Description description	ACTIN RELATED PROTEIN 11
Molecular weight formula_weight	46250.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J

MPLYEGLGSGGEKTAVVIDLGEAFTKCGFAGETGPRCIIPSVIKKAGMPKPIKVVQYNINTEELYSYLKEFIHILYFRHLLVNPRDRRVVVIESVLCPSHFRETLTRVLFKYFEVPSVLLAPSHLMALLTLGINSAMVLDCGYRESLVLPIYEGIPVLNCWGALPLGGKALHKELETQLLEQCTVDTGAAKEQSLPSVMGSIPEGVLEDIKVRTCFVSDLTRGLKIQAAKFNIDGNTERPSPPPNVDYPLDGEKILHVLGSIRDSVVEILFEQDNEEKSVATLILDSLMQCPIDTRKQLAENLVIIGGTSMLPGFLHRLLAEIRYLVEKPKYKKTLGTKTFRIHTPPAKANCVAWLGGAIFGALQDILGSRSVSKEYYNQTGRIPDWCSLNNPPLEMVFDVGKSQPPLMKRAFSTEK

Entity 4 Entity 4 polymer

Description description	CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1
Molecular weight formula_weight	31777.5 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	K

RVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVKIEGYEDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEEVDGSLKSWRESCDSALRAYVKDHYSNGFCTVYAKNIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSVTVSNEAQTAKEFIKIIEHAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGK

Entity 5 Entity 5 polymer

Description description	F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II
Molecular weight formula_weight	30509.5 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L

SDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLLCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYLWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNKSGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVNGLRSVDVIPDNPKFQQLQRELSQVLTQRQI

Entity 6 Entity 6 polymer

Description description	DYNACTIN SUBUNIT 2
Molecular weight formula_weight	70144.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Entity 7 Entity 7 polymer

Description description	DYNACTIN SUBUNIT 2
Molecular weight formula_weight	69633.5 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	N

Entity 8 Entity 8 polymer

Description description	DYNACTIN SUBUNIT 3
Molecular weight formula_weight	7507.2 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	O,P

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Entity 9 Entity 9 polymer

Description description	DYNACTIN SUBUNIT 2
Molecular weight formula_weight	7762.6 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Q,R

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Entity 10 Entity 10 polymer

Description description	DYNACTIN 5
Molecular weight formula_weight	20703.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	U

MAEKTQKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIVIGEGNLIEEQALIINAHPDNITPDAEDSEPKPMIIGTNNVFEVGCYSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCNLNTFEVIPENTVIYGADCLRRVQTERPQPQTLQLDFLMKILPNYHHLKKTMKGSSTPVKN

Entity 11 Entity 11 polymer

Description description	DYNACTIN SUBUNIT 6
Molecular weight formula_weight	18164.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	V

SGNKVSRQSVLCGSQNIVLNGKTIVMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSYYQKFLPLTQV

Entity 12 Entity 12 polymer

Description description	DYNACTIN SUBUNIT 2
Molecular weight formula_weight	20698.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Y

Entity 13 Entity 13 polymer

Description description	DYNACTIN SUBUNIT 2
Molecular weight formula_weight	35676.9 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Z,z

Entity 14 Entity 14 polymer

Description description	DYNACTIN SUBUNIT 2
Molecular weight formula_weight	5400.0 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	a

MADPKYADLPGIARNEPDVYLEELTSTSVEHAIVNPNAAYDKFKDKRV

Entity 15 Entity 15 polymer

Description description	DYNACTIN SUBUNIT 2
Molecular weight formula_weight	7931.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	b

MADPKYADLPGIARNEPDVYLEELTSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGE

Entity 16 Entity 16 polymer

Description description	DYNACTIN SUBUNIT 2
Molecular weight formula_weight	3173.6 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	c

MADPKYADLPGIARNEPDVYXXXXXXXXXXX

Entity 17 Entity 17 polymer

Description description	DYNACTIN SUBUNIT 2
Molecular weight formula_weight	2237.5 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	d

MADPKYADLPGIARNEPDVY

▼

6. Fold Classification (SCOP + CATH) 34 domains

CATH v4.4 (34 domains)

Domain ID domain_id	5adxA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxA03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — ATPase, substrate binding domain, subdomain 4

Domain ID domain_id	5adxB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxB03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — ATPase, substrate binding domain, subdomain 4

Domain ID domain_id	5adxC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxC03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — ATPase, substrate binding domain, subdomain 4

Domain ID domain_id	5adxD01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxD02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxD03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — ATPase, substrate binding domain, subdomain 4

Domain ID domain_id	5adxE01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxE02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxE03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — ATPase, substrate binding domain, subdomain 4

Domain ID domain_id	5adxF01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxF02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxF03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — ATPase, substrate binding domain, subdomain 4

Domain ID domain_id	5adxG01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxG02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxG03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — ATPase, substrate binding domain, subdomain 4

Domain ID domain_id	5adxH01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxH02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxH03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — ATPase, substrate binding domain, subdomain 4

Domain ID domain_id	5adxI01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxI02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	5adxI03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — ATPase, substrate binding domain, subdomain 4

Domain ID domain_id	5adxJ01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — ATPase, substrate binding domain, subdomain 4

Domain ID domain_id	5adxK01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1140 — Ribosomal protein S3 C-terminal domain
Homologous superfamily homologous superfamily	60 — F-actin capping protein, alpha subunit

Domain ID domain_id	5adxK02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily	210 — F-actin capping protein, beta subunit

Domain ID domain_id	5adxL01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	570 — F-actin capping protein, alpha/beta subunit, N-terminal domain

Domain ID domain_id	5adxL02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily	210 — F-actin capping protein, beta subunit

Domain ID domain_id	5adxU00
Class class	2 — Mainly Beta
Architecture architecture	160 — 3 Solenoid
Topology topology	10 — UDP N-Acetylglucosamine Acyltransferase; domain 1
Homologous superfamily homologous superfamily	10 — Hexapeptide repeat proteins

Domain ID domain_id	5adxV00
Class class	2 — Mainly Beta
Architecture architecture	160 — 3 Solenoid
Topology topology	10 — UDP N-Acetylglucosamine Acyltransferase; domain 1
Homologous superfamily homologous superfamily	10 — Hexapeptide repeat proteins

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	4.000 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	4.00 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	115044

CryoEM structure of dynactin complex at 4.0 angstrom resolution

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

ACTIN RELATED PROTEIN 1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

ACTIN, CYTOPLASMIC 1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

ACTIN RELATED PROTEIN 11

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

DYNACTIN 5

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5adx__assembly_1__model_1

5adx__assembly_1__model_1 | I(q)

5adx__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (17)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

Entity 6 Entity 6 polymer

Polymer Polymer

Entity 7 Entity 7 polymer

Polymer Polymer

Entity 8 Entity 8 polymer

Polymer Polymer

Entity 9 Entity 9 polymer

Polymer Polymer

Entity 10 Entity 10 polymer