8iai

Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State II, Global map

Method: ELECTRON MICROSCOPY D_max: 310.4 Å Quality: GOOD

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

Adducin 1

OrganismNot specified

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 1； UniProt 11–754 Chain 2； UniProt 11–754 Chain 9； UniProt 11–754	Not recorded	Beta-adducin × 2 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Actin, cytoplasmic 1 × 11 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 1 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADP ADENOSINE-5'-DIPHOSPHATE × 11	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 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.

Other PDB	Difference from Current Entry 8IAI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8IAH Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State I, Global map Deposited 2023-02-08	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 0 11–754（744 aa） Chain 1 11–754（744 aa） Chain 2 11–754（744 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A8D1Q0D0_PIG
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 1–744； UniProt 11–754 Author chain 2； PDBConstruct 1–744； UniProt 11–754 Author chain 9； PDBConstruct 1–744； UniProt 11–754

Beta-adducin

OrganismNot specified

UniProt A0A480JMR2

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 3； UniProt 1–724 Chain 4； UniProt 1–724	Not recorded	Adducin 1 × 3 （A0A8D1Q0D0） Dematin actin binding protein × 3 （A0A8D1E7W3） Actin, cytoplasmic 1 × 11 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 1 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADP ADENOSINE-5'-DIPHOSPHATE × 11	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8IAI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8IAH Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State I, Global map Deposited 2023-02-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 3 1–724（724 aa） Chain 4 1–724（724 aa） Chain 9 1–724（724 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A480JMR2_PIG
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain 3； PDBConstruct 1–724； UniProt 1–724 Author chain 4； PDBConstruct 1–724； UniProt 1–724

Dematin actin binding protein

OrganismNot specified

UniProt A0A8D1E7W3

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 5； UniProt 1–405 Chain 6； UniProt 1–405 Chain 7； UniProt 1–405	Not recorded	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 2 （A0A480JMR2） Actin, cytoplasmic 1 × 11 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 1 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADP ADENOSINE-5'-DIPHOSPHATE × 11	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8IAI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8IAH Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State I, Global map Deposited 2023-02-08	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 5 1–405（405 aa） Chain 6 1–405（405 aa） Chain 7 1–405（405 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
8IB2 Structure of mammalian spectrin-actin junctional complex of membrane skeleton, Pointed-end segment, headpiece domain of dematin optimized Deposited 2023-02-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain 5 1–405（405 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A8D1E7W3_PIG
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain 5； PDBConstruct 1–405； UniProt 1–405 Author chain 6； PDBConstruct 1–405； UniProt 1–405 Author chain 7； PDBConstruct 1–405； UniProt 1–405

Actin, cytoplasmic 1

OrganismNot specified

UniProt Q6QAQ1

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 31 PDB declaration: 31-meric（31） Consistent with protein copy count	Chain A； UniProt 1–375 Chain B； UniProt 1–375 Chain C； UniProt 1–375 Chain D； UniProt 1–375 Chain E； UniProt 1–375 Chain F； UniProt 1–375 Chain G； UniProt 1–375 Chain H； UniProt 1–375 Chain I； UniProt 1–375 Chain J； UniProt 1–375 Chain K； UniProt 1–375	Not recorded	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 2 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 1 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADP ADENOSINE-5'-DIPHOSPHATE × 11	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8IAI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5ADX CryoEM structure of dynactin complex at 4.0 angstrom resolution Deposited 2015-08-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric	Chain H 6–375（370 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT；pH 6.5；50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT cryo-EM vitrification conditions Cryogen ETHANE；LIQUID ENTHANE	Resolution 4.00 Å
5AFU Cryo-EM structure of dynein tail-dynactin-BICD2N complex Deposited 2015-01-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 33 PDB declaration: 33-meric	Chain H 6–375（370 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer 150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT；pH 7.4；150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT cryo-EM vitrification conditions Cryogen ETHANE；LIQUID ETHANE	Resolution 8.20 Å
6F1T Cryo-EM structure of two dynein tail domains bound to dynactin and BICDR1 Deposited 2017-11-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 45 PDB declaration: 45-meric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
6F38 Cryo-EM structure of two dynein tail domains bound to dynactin and HOOK3 Deposited 2017-11-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 45 PDB declaration: 45-meric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.70 Å
6F3A Cryo-EM structure of a single dynein tail domain bound to dynactin and BICD2N Deposited 2017-11-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.20 Å
6ZNL Cryo-EM structure of the dynactin complex Deposited 2020-07-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 23 PDB declaration: 23-meric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
6ZNM The pointed end complex of dynactin bound to BICDR1 Deposited 2020-07-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å
6ZNN The pointed end complex of dynactin bound to Hook3 Deposited 2020-07-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å
6ZNO The pointed end complex of dynactin with the p150 projection docked Deposited 2020-07-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.80 Å
6ZO4 The pointed end complex of dynactin bound to BICD2 Deposited 2020-07-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 8.20 Å
7Z8F Composite structure of dynein-dynactin-BICDR on microtubules Deposited 2022-03-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 43 PDB declaration: 43-meric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 13 MG MAGNESIUM ION × 14 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ZN ZINC ION × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE；20 second incubation	Resolution 20.00 Å
7Z8M The pointed end complex of dynactin bound to BICDR1 Deposited 2022-03-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain H 1–375（375 aa）	Not recorded	ZN ZINC ION × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE；20 second incubation	Resolution 3.37 Å
8IAH Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State I, Global map Deposited 2023-02-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain A 1–375（375 aa） Chain B 1–375（375 aa） Chain C 1–375（375 aa） Chain D 1–375（375 aa） Chain E 1–375（375 aa） Chain F 1–375（375 aa） Chain G 1–375（375 aa） Chain H 1–375（375 aa） Chain I 1–375（375 aa） Chain J 1–375（375 aa） Chain K 1–375（375 aa） Chain L 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
8IB2 Structure of mammalian spectrin-actin junctional complex of membrane skeleton, Pointed-end segment, headpiece domain of dematin optimized Deposited 2023-02-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–375（375 aa） Chain C 1–375（375 aa） Chain D 1–375（375 aa） Chain E 1–375（375 aa） Chain F 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8P94 Cryo-EM structure of cortactin stabilized Arp2/3-complex nucleated actin branches Deposited 2023-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain H 1–375（375 aa） Chain J 1–375（375 aa） Chain K 1–375（375 aa） Chain N 1–375（375 aa） Chain O 1–375（375 aa） Chain P 1–375（375 aa） Chain Q 1–375（375 aa） Chain R 1–375（375 aa） Chain S 1–375（375 aa） Chain W 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions Cryogen ETHANE；Back blotting	Resolution 3.30 Å
8PTK Composite structure of Dynein-Dynactin-JIP3-LIS1 Deposited 2023-07-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 53 PDB declaration: 53-meric	Chain H 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 16 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ZN ZINC ION × 3 MG MAGNESIUM ION × 6 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 10.00 Å
9DGR Composite structure of dynein-dynactin on microtubules Deposited 2024-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 39 PDB declaration: 39-meric	Chain H 1–375（375 aa）	Not recorded	ZN ZINC ION × 3 MG MAGNESIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 15.00 Å
9DGS Dynactin and dynein tail region of dynein-dynactin complex on microtubules Deposited 2024-09-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 31 PDB declaration: 31-meric	Chain H 1–375（375 aa）	Not recorded	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 3.90 Å
9DGT structure of dynactin, dynein tail with one BICDR from dynein-dynactin-BICDR on microtubules Deposited 2024-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 35 PDB declaration: 35-meric	Chain H 1–375（375 aa）	Not recorded	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 7.20 Å
9DGU structure of dynactin, dynein tail with two BICDR from dynein-dynactin-BICDR on microtubules Deposited 2024-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 37 PDB declaration: 37-meric	Chain H 1–375（375 aa）	Not recorded	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 7.10 Å
9DGV structure of dynactin, dynein tail with TRAK2 from dynein-dynactin-TRAK2 on microtubules Deposited 2024-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 33 PDB declaration: 33-meric	Chain H 1–375（375 aa）	Not recorded	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 8.80 Å
9HHL Structure of Dynein-Dynactin-NuMA-LIS1 Deposited 2024-11-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 41 PDB declaration: 41-meric	Chain H 1–375（375 aa）	Not recorded	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
9I2B SPIN90-Arp2/3 nucleated bidirectional actin filaments Deposited 2025-01-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain I 1–375（375 aa） Chain J 1–375（375 aa） Chain S 1–375（375 aa） Chain T 1–375（375 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 8 MG MAGNESIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9YNG Dynactin and dynein-1 tail region of dynein-dynactin complex on microtubule in the presence of LIS1 Deposited 2025-10-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 31 PDB declaration: 31-meric	Chain H 1–375（375 aa）	Not recorded	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

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 A； PDBConstruct 1–375； UniProt 1–375 Author chain B； PDBConstruct 1–375； UniProt 1–375 Author chain C； PDBConstruct 1–375； UniProt 1–375 Author chain D； PDBConstruct 1–375； UniProt 1–375 Author chain E； PDBConstruct 1–375； UniProt 1–375 Author chain F； PDBConstruct 1–375； UniProt 1–375 Author chain G； PDBConstruct 1–375； UniProt 1–375 Author chain H； PDBConstruct 1–375； UniProt 1–375 Author chain I； PDBConstruct 1–375； UniProt 1–375 Author chain J； PDBConstruct 1–375； UniProt 1–375 Author chain K； PDBConstruct 1–375； UniProt 1–375

Spectrin beta chain

OrganismNot specified

UniProt A0A480J001

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 1–2148 Chain N； UniProt 1–2148 Chain O； UniProt 1–2148 Chain P； UniProt 1–2148 Chain Q； UniProt 1–2148 Chain R； UniProt 1–2148 Chain S； UniProt 1–2148 Chain T； UniProt 1–2148	Not recorded	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 2 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Actin, cytoplasmic 1 × 11 （Q6QAQ1） Tropomyosin-1.9 × 1 Tropomyosin 3 × 1 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADP ADENOSINE-5'-DIPHOSPHATE × 11	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8IAI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8IAH Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State I, Global map Deposited 2023-02-08	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain M 1–2148（2148 aa） Chain N 1–2148（2148 aa） Chain O 1–2148（2148 aa） Chain P 1–2148（2148 aa） Chain Q 1–2148（2148 aa） Chain R 1–2148（2148 aa） Chain S 1–2148（2148 aa） Chain T 1–2148（2148 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A480J001_PIG
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain M； PDBConstruct 1–2148； UniProt 1–2148 Author chain N； PDBConstruct 1–2148； UniProt 1–2148 Author chain O； PDBConstruct 1–2148； UniProt 1–2148 Author chain P； PDBConstruct 1–2148； UniProt 1–2148 Author chain Q； PDBConstruct 1–2148； UniProt 1–2148 Author chain R； PDBConstruct 1–2148； UniProt 1–2148 Author chain S； PDBConstruct 1–2148； UniProt 1–2148 Author chain T； PDBConstruct 1–2148； UniProt 1–2148

Tropomyosin 3

OrganismNot specified

UniProt Q6QA25

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 1–248	Not recorded	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 2 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Actin, cytoplasmic 1 × 11 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADP ADENOSINE-5'-DIPHOSPHATE × 11	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8IAI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8IAH Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State I, Global map Deposited 2023-02-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain V 1–248（248 aa） Chain W 1–248（248 aa） Chain X 1–248（248 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q6QA25_PIG
Isoform	—
PDB entities	7
Chains and sequence ranges	Author chain V； PDBConstruct 1–248； UniProt 1–248

Tropomodulin-1

OrganismNot specified

UniProt A0A287BCZ0

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 1–359	Not recorded	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 2 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Actin, cytoplasmic 1 × 11 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 1 （Q6QA25） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADP ADENOSINE-5'-DIPHOSPHATE × 11	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8IAI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8IAH Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State I, Global map Deposited 2023-02-08	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain Y 1–359（359 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A287BCZ0_PIG
Isoform	—
PDB entities	8
Chains and sequence ranges	Author chain Y； PDBConstruct 1–359； UniProt 1–359

SH3 domain-binding glutamic acid-rich-like protein

OrganismNot specified

UniProt A0A4X1V2Q0

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 Z； UniProt 1–107	Not recorded	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 2 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Actin, cytoplasmic 1 × 11 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 1 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） ADP ADENOSINE-5'-DIPHOSPHATE × 11	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8IAI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8IAH Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State I, Global map Deposited 2023-02-08	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain Z 1–107（107 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A4X1V2Q0_PIG
Isoform	—
PDB entities	9
Chains and sequence ranges	Author chain Z； PDBConstruct 1–107； UniProt 1–107

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	8iai
Deposition date deposition_date	2023-02-08
Structure title title	Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State II, Global map
Keywords keywords	Macrocomplex, membrane skeleton, spectrin-actin junction, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	— Å
Radius of gyration Rg (electron density) rg_electron	116.50 Å
Forward intensity I(0) i0	10369100000.00
Molecular weight molecular_weight	859650.0 kDa
Excluded volume excluded_volume	1074100 Å³
Envelope volume envelope_volume	1807900 Å³
Hydration-shell volume shell_volume	156200 Å³
Envelope diameter envelope_diameter	426.1 Å
Shell Rg shell_rg	70.71 Å
Envelope Rg envelope_rg	117.50 Å
Shape Rg shape_rg	116.50 Å
Total Rg total_rg	115.90 Å
Total atoms total_atoms	60300
Residues n_residues	7612
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	310.4 Å
Rg (real space) rg_real	103.30 Å
Rg uncertainty (real space) rg_real_error	2.31 Å
I(0) (real space) i0_real	9.9190e+09
I(0) uncertainty (real space) i0_real_error	2.4010e+08
Rg (reciprocal space) rg_reciprocal	93.33 Å
I(0) (reciprocal space) i0_reciprocal	9774000000.0000
Solution quality estimate total_estimate	0.8782
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	71.6 Å
Skewness Skewness skewness	0.460
Kurtosis Kurtosis kurtosis	-0.771
Angular range angular_range	— – 0.0650 Å⁻¹
Current regularization parameter α current_alpha	0.3741
Highest regularization parameter α highest_alpha	127900000.0000
Real-space data points n_real_points	14
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.012; Oscil: 0.827; Stabil: 0.990; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.030

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (10)

Entity 1 Entity 1 polymer

Description description	Adducin 1
Molecular weight formula_weight	81307.2 kDa
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1,2,9
Atom count atom_count	60300

MNGDTRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTTNVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAALYRLADLFGWSHLIYNHITTRVSSEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDRGSTNLGVNQAGFTLHSAVYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGEVAYHDYHGILVDEEEKVLIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGGPDNLVLLDPGKYKAKSRPPTSPAGEGSGSPPAWQIGEQEFEALMRMLDNLGYRTGYPYRYPALREKSKKYSDVEVPASVTGYSVASDGDSGTGSPLRHSFQKQQREKTRWLNSGRGDDASEEGQAGSSPKSKTKWTKEDGHRASASAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVVMDRSLVQGELVTASKAIIEKEYQPHVVVSTTGPNPFNTLTDRELEEYRREVERKQKGPEETLDERSDQKEDSPPEPPAAPHTPPSTPVKLEEDLPQEPLSGDDSEAATFRPTLPDLPPDEPSEVLGFPTLEEEEEEEEVGALCEAGRPPSPARPAAEASPEPAAAQAAEEPASPAAEEGAAADPGSDGSPGKSPSKKKKKFRTPSFLKKSKKRSDS

Entity 2 Entity 2 polymer

Description description	Beta-adducin
Molecular weight formula_weight	80705.9 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

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

MSEETVPEAASPPPAQGRQYFDRFSEEDPEYLRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPTSSMNFSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFCLHSAIYAARPDVRCIIHLHTPATAAVSAMKWGLLPVSHNALLVGDMAYFDFNGEMEQEADRINLQKCLGPTCKILVLRNHGVVALGDTVEEAFYKVFHLQAACEIQVSALSSAGGVENLILLEQEKHRPHEVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYPYRYPLVQEKTKHKSEVEIPATVTAFVFEEDGAPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRSMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLDMRNKIREQNRQDVKSAGPQSQLLASVIAEKSRSPSTESQLMSQGQADTKDESEETVPNPFSQLTDQELEEYKKEVERKKLELDGEKEPAVEEPGSPGKSAPASPAQSPAKSETKSPVGSPSKSVDEEAQKTEPSKPTTEPETTQPEGVVVNGREDEPTAEEILSKGLSQMTTHADTDVDTSKDKTESVTSGPMSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES

Entity 3 Entity 3 polymer

Description description	Dematin actin binding protein
Molecular weight formula_weight	45569.3 kDa
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	5,6,7

MERLQKQPLTSPGSVSSSRGSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPRSRERSLSPKSTSPPPSPEVWAESRSPGTFPQASAPRTTGTPRTSLPHFHHPETTRPDSNIYKKPPIYKQREPTGGSPQSKHLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLQAGTSKSSSLPAYGRTTLSRLQSTDFSPSGSETESPGLQNGEGQRGRMDRGTSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFSMSPEEFGKLALWKRNELKKKASLF

Entity 4 Entity 4 polymer

Description description	Actin, cytoplasmic 1
Molecular weight formula_weight	41782.7 kDa
Source method src_method	nat
Copy count entity_count	11

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K

MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

Entity 5 Entity 5 polymer

Description description	Spectrin beta chain
Molecular weight formula_weight	248510.7 kDa
Source method src_method	nat
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M,N,O,P,Q,R,S,T

MTSATEFENVGNQPPYSRINARWDAPDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQEGRETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFDVAERQLGIIQLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQTITVLNSRKFANSLAGVQQQLQAFSTYRTVEKPPKFQEKGNLEVLLFTIQSRMRANNQKVYTPHDGKLVSDINRAWESLEEAEYRRELALRSELIRQEKLEQLARRFDRKAAMRETWLNENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLARELELENYHDQKRITARKDNILRLWNYLQELLQSRRQRLETTLALQQLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEAEDLLQKHKLMEADIAIQGDKVKAITAATLQFTEETGYQPCDPQVIRDRVSHLEQCFAELSNTAAGRKAQLEQSKRLWKLFWEMDEAKSWIKEKEQIYSSLGYGKDLTSVLILQRKHKAFEDELRRLDPHLDQIFQEAEDMVALKQFGYPKNEAWVKEVSAQWDQLKEVPAQWNQLKELAASRKKNLQDTENFFQFQGDVDDLKAWLQDAHKLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQDFPERFRDSPDVTNRLQVLRDLYQQVVAQADLRRQRLQDALDLYTVFGETDACELWMGEKEKWLAQMDIPDTLEDLEVVQHRFDILDQEMKTLIAQIDGVNVAANSLVESNHPRSTEVKQYQDHLNTRWREFQTMVLARREAVDSALRVHNYCVDCEETSKWIIDKTKVVESTKDLGQDLAGVMAIQRKLSGLERDVAAIQVRVGALEQESHRLMESHREQEKDIGERQAYVEELWQGLQQALKGQEALLGKSSQLQAFLQDLDAFEAWLSTAQKEVASKDMPESLPEAEQLLQQHAALKDDIDRHQENYQHVKASGEKVIHGQTDPEYLLLGQRLEGLDKGWDALCRMWESRGHTLAQCLGFQEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFQDFFTTMENNRDKVLSPVDSGNKLVAEGNLYSDKIKEKVQQIEDRHKRNNEKAQEASVLLQDNLALQNFLQNCQELTLWINDKLLTSQDVSYDDARNLHNKWLKHTAFEAELASQQGWLENIDAEGKQLMEEKPQFEALVSQRLEALHRLWDELQATTKEIGQRLSAARSSDLRSQTHADLNKWIRAMEDQLRSDDLGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAHMPSPGEEAEDEDLSIEKRFLDLLEPLGRRKKQLESSKAKLQISRDLEDETLWVEERLPLAQSTDYGANLQTVQLFMKKNQTLQNEILGHAPRVEDVLYRGHQLVEAAEIDCQDIEERLGHLQNSWDTLQEAAAGRLQRLWDASEAQQYYLDAGEAEAWISEQELYVISDEMPQDEEGAIVMLKRHLRQQRMVEEYERNIKQLAGRAQSLLAAGHPEGEQIIRLQGQVDKHYAGLKDMAEDRKRKLENKYRQFQMEREADDLEQWILEKDLVASSPEMGQDFDHVTLLRDKFRDFARETGAIGQERVDNMNALIEHLIDAGHEEAASIAERKDGLNEMWADVLELIDTRMQLLAASYDRHRYFYTGNEILGLIDEKHRELPEDVGLDASTAESFHRVHTAFERELHQLGVQVQQFQDVATRLQAAYAGEEADSIQNKEQEVSAAWQALLDACAGRRTQLVDTADKFRFFSMVRDLLSWMETIIRQIETQERPRDVSSVELLMKYHQGIWAEMDTRSKNFSACLELGESLLQRQHQASDEIREKLQQVVSKKKEIDEKWKARSDRLSMLLEVCQFSRDASVAEAWLIAQEPYLSSRDFGHTVDSVEKLIKRHEAFEKSTASWEPRFAALEKPTTLELKERQTPERPKEDAGPQEEEGETAGEAPRGPHRAATERTSPVSSLSHLSSSWESLLPEPAHPY

Entity 6 Entity 6 polymer

Description description	Tropomyosin-1.9
Molecular weight formula_weight	28791.2 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	U

MAGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDYERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNNM

Entity 7 Entity 7 polymer

Description description	Tropomyosin 3
Molecular weight formula_weight	29080.7 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	V

MAGITTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEEHLCTQRMLDQTLLDLNEM

Entity 8 Entity 8 polymer

Description description	Tropomodulin-1
Molecular weight formula_weight	40523.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Y

MSYRRELEKYRDLDEDEILGALTEEELRTLENELDELDPDNALLPAGLRQKDQTTKAPTGPFKREELLDHLEKQAKEFKDREDLVPYTGEKRGKVWVPKQKPMDPVLETVTLEPELEEALANASDAELCDIAAILGMHTLMSNQQYYQALGSSSIVNKEGLNSVIKPTQYKPVPDEEPNATDVEETLERIKNNDPKLEEVNLNNIRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILRLVEALPYNTSLVELKIDNQSQPLGNKVEMEIVSMLEKNATLLKFGYHFTQQGPRLRASNAMMNNNDLVRKRRLADLTGPIIPKCRSGI

Entity 9 Entity 9 polymer

Description description	SH3 domain-binding glutamic acid-rich-like protein
Molecular weight formula_weight	12285.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Z

MVIRVFIASSSGFVAIKKKQQDVVRFLEANKIEFEEVDITMSEEQRQWMYKNIPPEKKPAQGNPLPPQIFNGDRYCGDYDSFFESKESNTVFSFLGLKSQLASKAEP

Entity 10 Entity 10 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	11

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7. Fold Classification (SCOP + CATH) 11 domains

CATH v4.4 (11 domains)

Domain ID domain_id	8iaiA01
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	8iaiB01
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	8iaiC01
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	8iaiD01
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	8iaiE01
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	8iaiF01
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	8iaiG01
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	8iaiH01
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	8iaiI01
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	8iaiJ01
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	8iaiK01
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

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8. Citations (1)

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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	—

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

Resolution resolution	3.50 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	68000

fit	/app/data/saxs_computation/ia/8iai/8iai.fit
pddf	/app/data/pr_computation/ia/8iai/8iai.pr.out
profile	/app/data/saxs_computation/ia/8iai/8iai.dat

Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State II, Global map

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

Adducin 1

State in the Current Structure

Other States of the Same Protein in the Database

Beta-adducin

State in the Current Structure

Other States of the Same Protein in the Database

Dematin actin binding protein

State in the Current Structure

Other States of the Same Protein in the Database

Actin, cytoplasmic 1

State in the Current Structure

Other States of the Same Protein in the Database

Spectrin beta chain

State in the Current Structure

Other States of the Same Protein in the Database

Tropomyosin 3

State in the Current Structure

Other States of the Same Protein in the Database

Tropomodulin-1

State in the Current Structure

Other States of the Same Protein in the Database

SH3 domain-binding glutamic acid-rich-like protein

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (10)

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 non-polymer

7. Fold Classification (SCOP + CATH) 11 domains

CATH v4.4 (11 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)