5afu

Cryo-EM structure of dynein tail-dynactin-BICD2N complex

Method: ELECTRON MICROSCOPY

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

DYNACTIN

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 33	DYNEIN TAIL × 1 DYNEIN TAIL × 1 DYNEIN TAIL × 2 DYNEIN TAIL × 2 ACTIN, CYTOPLASMIC 1 × 1 （Q6QAQ1） DYNACTIN × 1 （I3LHK5） CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 （A0PFK5） F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 （D2JYW4） DYNACTIN × 1 DYNACTIN 6 × 1 DYNACTIN × 2 DYNACTIN × 2 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 ADENOSINE-5'-DIPHOSPHATE × 9 ADENOSINE-5'-TRIPHOSPHATE × 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	5
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 33	DYNEIN TAIL × 1 DYNEIN TAIL × 1 DYNEIN TAIL × 2 DYNEIN TAIL × 2 DYNACTIN × 8 （F2Z5G5） DYNACTIN × 1 （I3LHK5） CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 （A0PFK5） F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 （D2JYW4） DYNACTIN × 1 DYNACTIN 6 × 1 DYNACTIN × 2 DYNACTIN × 2 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 ADENOSINE-5'-DIPHOSPHATE × 9 ADENOSINE-5'-TRIPHOSPHATE × 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	6
Chains and sequence ranges	Author chain H； PDBConstruct 1–370； UniProt 6–375

DYNACTIN

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 33	DYNEIN TAIL × 1 DYNEIN TAIL × 1 DYNEIN TAIL × 2 DYNEIN TAIL × 2 DYNACTIN × 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 × 1 DYNACTIN 6 × 1 DYNACTIN × 2 DYNACTIN × 2 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 ADENOSINE-5'-DIPHOSPHATE × 9 ADENOSINE-5'-TRIPHOSPHATE × 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	7
Chains and sequence ranges	Author chain J； PDBConstruct 1–379； UniProt 12–390

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 33	DYNEIN TAIL × 1 DYNEIN TAIL × 1 DYNEIN TAIL × 2 DYNEIN TAIL × 2 DYNACTIN × 8 （F2Z5G5） ACTIN, CYTOPLASMIC 1 × 1 （Q6QAQ1） DYNACTIN × 1 （I3LHK5） F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 （D2JYW4） DYNACTIN × 1 DYNACTIN 6 × 1 DYNACTIN × 2 DYNACTIN × 2 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 ADENOSINE-5'-DIPHOSPHATE × 9 ADENOSINE-5'-TRIPHOSPHATE × 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	8
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 33	DYNEIN TAIL × 1 DYNEIN TAIL × 1 DYNEIN TAIL × 2 DYNEIN TAIL × 2 DYNACTIN × 8 （F2Z5G5） ACTIN, CYTOPLASMIC 1 × 1 （Q6QAQ1） DYNACTIN × 1 （I3LHK5） CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 （A0PFK5） DYNACTIN × 1 DYNACTIN 6 × 1 DYNACTIN × 2 DYNACTIN × 2 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 ADENOSINE-5'-DIPHOSPHATE × 9 ADENOSINE-5'-TRIPHOSPHATE × 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	9
Chains and sequence ranges	Author chain L； PDBConstruct 1–270； UniProt 2–271

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	5afu
Deposition date deposition_date	2015-01-26
Structure title title	Cryo-EM structure of dynein tail-dynactin-BICD2N complex
Keywords keywords	DYNEIN, DYNACTIN, BICD2, MOTOR, TRANSPORT, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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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.

5afu__assembly_1__model_1

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

Download this curve (.dat)

5afu__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5afu__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	96.22 Å
Rg (electron density)	97.59 Å
Total Rg	97.09 Å
Atom count	55952
Residues	8572
Excluded volume	964020 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5afu__assembly_1__model_1`	33-meric （33）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (24)

Entity 1 Entity 1 polymer

Description description	DYNEIN TAIL
Molecular weight formula_weight	30740.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1
Atom count atom_count	55952

Entity 2 Entity 2 polymer

Description description	DYNEIN TAIL
Molecular weight formula_weight	30570.6 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	2

Entity 3 Entity 3 polymer

Description description	DYNEIN TAIL
Molecular weight formula_weight	38900.7 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	3,4

HYLVPYNQRANHSKPIPPFLLDLDSQSVPDALKKQTNDYYILYNPALPREIDVELHKSLDHTSVVCCVKFSNDGEYLATGCNKTTQVYRVSDGSLVARLSDSSDLYIRSVCFSPDGKFLATGAEDRLIRIWDIENRKIVMILQGHEQDIYSLDYFPSGDKLVSGSGDRTVRIWDLRTGQCSLTLSIEDGVTTVAVSPGDGKYIAAGSLDRAVRVWDSETGFLVERLDTGHKDSVYSVVFTRDGQSVVSGSLDRSVKLWNLTCEVTYIGHKDFVLSVATTQNDEYILSGSKDRGVLFWDKKSGNPLLMLQGHRNSVISVAVANGSSLGPEYNVFATGSGDCKARIWKYKKI

Entity 4 Entity 4 polymer

Description description	DYNEIN TAIL
Molecular weight formula_weight	23421.8 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	5,6

Entity 5 Entity 5 polymer

Description description	DYNACTIN
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

IANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHVRVMAGALEGDIFIGPKAEEHRGLLSIRYPMEHGIVKDWNDMERIWQYVYSKEQLQTFSEEHPVLLTEAPLNPRKNRERAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRIDIAGRDVSRFLRLYLRKEGYDFHSSSEFEIVKAIKERACYLSINPQKDETLETEKAQYYLPDGSTIEIGPSRFRAPELLFRPDLIGEESEGIHEVLVFAIQKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGARSIHRKTF

Entity 6 Entity 6 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 7 Entity 7 polymer

Description description	DYNACTIN
Molecular weight formula_weight	42141.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J

EKTAVVIDLGEAFTKCGFAGETGPRCIIPSVIKKAGMPKPIKVVQYNINTEELYSYLKEFIHILYFRHLLVNPRDRRVVVIESVLCPSHFRETLTRVLFKYFEVPSVLLAPSHLMALLTLGINSAMVLDCGYRESLVLPIYEGIPVLNCWGALPLGGKALHKELETQLLEQCTVDTGAAKEQSLPSVMGSIPEGVLEDIKVRTCFVSDLTRGLKIQAAKFNIDGNTERPSPPPNVDYPLDGEKILHVLGSIRDSVVEILFEQDNEEKSVATLILDSLMQCPIDTRKQLAENLVIIGGTSMLPGFLHRLLAEIRYLVEKPKYKKTLGTKTFRIHTPPAKANCVAWLGGAIFGALQDILGSRSVSKEYYNQTGRIPDWCSL

Entity 8 Entity 8 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 9 Entity 9 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 10 Entity 10 polymer

Description description	DYNACTIN
Molecular weight formula_weight	49974.7 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Entity 11 Entity 11 polymer

Description description	DYNACTIN 6
Molecular weight formula_weight	52442.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	N

Entity 12 Entity 12 polymer

Description description	DYNACTIN
Molecular weight formula_weight	5549.8 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

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

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Entity 13 Entity 13 polymer

Description description	DYNACTIN
Molecular weight formula_weight	7422.1 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

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

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Entity 14 Entity 14 polymer

Description description	DYNACTIN
Molecular weight formula_weight	18343.2 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	U

PGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIVIGEGNLIEEQALIINAYPDNITPDTEKPMIIGTNNVFEVGCYSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCNLNTFEVIPENTVIYGADCLRRVQTERPQPTLQLDFLMKILPNYHHLKKTMKGSS

Entity 15 Entity 15 polymer

Description description	DYNACTIN
Molecular weight formula_weight	18178.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	V

SGNKVSRQSVLCGSQNIVLNGKTIIMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSYYQKFLPLTQV

Entity 16 Entity 16 polymer

Description description	F-ACTIN-CAPPING PROTEIN SUBUNIT BETA
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 17 Entity 17 polymer

Description description	F-ACTIN-CAPPING PROTEIN SUBUNIT BETA
Molecular weight formula_weight	4443.5 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Z

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Entity 18 Entity 18 polymer

Description description	DYNACTIN
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 19 Entity 19 polymer

Description description	DYNACTIN
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 20 Entity 20 polymer

Description description	DYNACTIN
Molecular weight formula_weight	3019.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	c

MADPKYADLPGIARNEPDVYAAAAAAAAAAA

Entity 21 Entity 21 polymer

Description description	DYNACTIN
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

Entity 22 Entity 22 polymer

Description description	F-ACTIN-CAPPING PROTEIN SUBUNIT BETA
Molecular weight formula_weight	4528.6 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	z

XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Entity 23 Entity 23 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 24 Entity 24 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	1

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6. Fold Classification (SCOP + CATH) 35 domains

CATH v4.4 (35 domains)

Domain ID domain_id	5afu300
Class class	2 — Mainly Beta
Architecture architecture	130 — 7 Propeller
Topology topology	10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily	10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

Domain ID domain_id	5afu400
Class class	2 — Mainly Beta
Architecture architecture	130 — 7 Propeller
Topology topology	10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily	10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

Domain ID domain_id	5afuA01
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	5afuA02
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	5afuA03
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	5afuB01
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	5afuB02
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	5afuB03
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	5afuC01
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	5afuC02
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	5afuC03
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	5afuD01
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	5afuD02
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	5afuD03
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	5afuE01
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	5afuE02
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	5afuE03
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	5afuF01
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	5afuF02
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	5afuF03
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	5afuG01
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	5afuG02
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	5afuG03
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	5afuH01
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	5afuH02
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	5afuH03
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	5afuI01
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	5afuI02
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	5afuI03
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	5afuK01
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	5afuK02
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	5afuL01
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	5afuL02
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	5afuU00
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	5afuV00
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	8.200 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	8.20 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	85744

Cryo-EM structure of dynein tail-dynactin-BICD2N complex

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

DYNACTIN

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

DYNACTIN

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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5afu__assembly_1__model_1

5afu__assembly_1__model_1 | I(q)

5afu__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 (24)

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

Polymer Polymer

Entity 11 Entity 11 polymer

Polymer Polymer

Entity 12 Entity 12 polymer

Polymer Polymer

Entity 13 Entity 13 polymer

Polymer Polymer

Entity 14 Entity 14 polymer