8iah

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

Method: ELECTRON MICROSCOPY

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

Adducin 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 36	Beta-adducin × 3 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Spectrin alpha, erythrocytic 1 × 1 （A0A5G2R924） Actin, cytoplasmic 1 × 12 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 3 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADENOSINE-5'-DIPHOSPHATE × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A8D1Q0D0_PIG
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 0； PDBConstruct 1–744； UniProt 11–754 Author chain 1； PDBConstruct 1–744； UniProt 11–754 Author chain 2； PDBConstruct 1–744； UniProt 11–754

Beta-adducin

OrganismNot specified

UniProt A0A480JMR2

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 36	Adducin 1 × 3 （A0A8D1Q0D0） Dematin actin binding protein × 3 （A0A8D1E7W3） Spectrin alpha, erythrocytic 1 × 1 （A0A5G2R924） Actin, cytoplasmic 1 × 12 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 3 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADENOSINE-5'-DIPHOSPHATE × 12	Consistent with protein count

Other States of the Same Protein in the Database

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 Author chain 9； PDBConstruct 1–724； UniProt 1–724

Dematin actin binding protein

OrganismNot specified

UniProt A0A8D1E7W3

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 36	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 3 （A0A480JMR2） Spectrin alpha, erythrocytic 1 × 1 （A0A5G2R924） Actin, cytoplasmic 1 × 12 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 3 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADENOSINE-5'-DIPHOSPHATE × 12	Consistent with protein count

Other States of the Same Protein in the Database

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

Spectrin alpha, erythrocytic 1

OrganismNot specified

UniProt A0A5G2R924

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 36	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 3 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Actin, cytoplasmic 1 × 12 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 3 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADENOSINE-5'-DIPHOSPHATE × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A5G2R924_PIG
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain 8； PDBConstruct 1–2417； UniProt 1–2417

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 36	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 3 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Spectrin alpha, erythrocytic 1 × 1 （A0A5G2R924） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 3 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADENOSINE-5'-DIPHOSPHATE × 12	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	5
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 Author chain L； PDBConstruct 1–375； UniProt 1–375

Spectrin beta chain

OrganismNot specified

UniProt A0A480J001

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 36	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 3 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Spectrin alpha, erythrocytic 1 × 1 （A0A5G2R924） Actin, cytoplasmic 1 × 12 （Q6QAQ1） Tropomyosin-1.9 × 1 Tropomyosin 3 × 3 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADENOSINE-5'-DIPHOSPHATE × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A480J001_PIG
Isoform	—
PDB entities	6
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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 36	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 3 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Spectrin alpha, erythrocytic 1 × 1 （A0A5G2R924） Actin, cytoplasmic 1 × 12 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomodulin-1 × 1 （A0A287BCZ0） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADENOSINE-5'-DIPHOSPHATE × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q6QA25_PIG
Isoform	—
PDB entities	8
Chains and sequence ranges	Author chain V； PDBConstruct 1–248； UniProt 1–248 Author chain W； PDBConstruct 1–248； UniProt 1–248 Author chain X； PDBConstruct 1–248； UniProt 1–248

Tropomodulin-1

OrganismNot specified

UniProt A0A287BCZ0

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 36	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 3 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Spectrin alpha, erythrocytic 1 × 1 （A0A5G2R924） Actin, cytoplasmic 1 × 12 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 3 （Q6QA25） SH3 domain-binding glutamic acid-rich-like protein × 1 （A0A4X1V2Q0） ADENOSINE-5'-DIPHOSPHATE × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A287BCZ0_PIG
Isoform	—
PDB entities	9
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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 36	Adducin 1 × 3 （A0A8D1Q0D0） Beta-adducin × 3 （A0A480JMR2） Dematin actin binding protein × 3 （A0A8D1E7W3） Spectrin alpha, erythrocytic 1 × 1 （A0A5G2R924） Actin, cytoplasmic 1 × 12 （Q6QAQ1） Spectrin beta chain × 8 （A0A480J001） Tropomyosin-1.9 × 1 Tropomyosin 3 × 3 （Q6QA25） Tropomodulin-1 × 1 （A0A287BCZ0） ADENOSINE-5'-DIPHOSPHATE × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A4X1V2Q0_PIG
Isoform	—
PDB entities	10
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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8iah
Deposition date deposition_date	2023-02-08
Structure title title	Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State I, Global map
Keywords keywords	Macrocomplex, membrane skeleton, spectrin-actin junction, MEMBRANE PROTEIN; MEMBRANE 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.

8iah__assembly_1__model_1

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

Download this curve (.dat)

8iah__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

8iah__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	0.00 Å
Rg (electron density)	119.30 Å
Total Rg	118.90 Å
Atom count	74320
Residues	9387
Excluded volume	1321300 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`8iah__assembly_1__model_1`	36-meric （36）	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 (11)

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	0,1,2
Atom count atom_count	74320

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	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	3,4,9

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	Spectrin alpha, erythrocytic 1
Molecular weight formula_weight	281361.0 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	8

MNAGNWSQAMDSGGPKVLETAEEIQERRQEVLSRYGKFKEQVAERGQKLEDSYHYQVFKRDADDLKKWILEKLKIAEDKSYEDPTNIQGKYQKHESFETEVQAKSRVIPELEEIRRVRFTEGHVAHEDTKVLLEELHTLWNRLLEWTQQKGSLLLQALKLQQYLQECADILEWIGDKEAIVTSEELGEDWERTEVLHKKFEEFQADLEIRRGRVNGVNQYADECVEENHPKLPLIQSRREEVNEAWERLNKLASQRQKSLSSVADLQRFKRDVTEAIQWIKEKEPQLTSEDYGKDLFTSEALFHSHKGLERNLAVMDDKVKELCAKADKLKLSHPSDADQIQQMKEDLVSNWEHIRTLATRRYEKLQASYWYQRFLSDYDELSGWMKEKTALINADELPTDVAGGEALLDRHQQHKHEIDSYDDRFQSAHETGQALLDANHEASDEVMEKMNILVHTRAALLELWNRRQQQYEQCLNLHLFYRDSEQVDSWMSRQEAFLENEDLGNSLGSVEALLQKHDDFEEAFTAQEEKITTLDETATKLIDDHHYDSKNIAAIRDELLARQDALRKRAATRRKLLEDSFLLQQLYQDSDDLKNWINKKKKLADDEDYKDTQNLKSQVQKQQVFEEELAANKILLDNLKQTGQEMIENNHYASERVAARLSDIDSLWRELLEATAQKGTQLYEANRLLQFENNAEDLQRWLEEVKWQAFSEDYGKGLADIQNLRRKHQLLESAVAARQDQADTLKDLAAHFEEIGHPNAGELRARQESLVSRFEELKEPLSFRKNKLNDQFMLLWICRDTEDEEAWIQETEPSAASTYLGKDLIAAKKFLSRHQVIQADIANHEPRIQEITWRGNKMVEEGHFAAEDVASRIKSLNENMESLQARAARRQNALEANVQFQQYLADLHEAEAWIREKEPIVDNTNYGADEEAAGALLKKHEAFLVDLKAFGNSIQALRDQAEACQQQQAAPVEADAREERVMALYDFEARSPREVTMKKDDILILLSSINEDWWKVEADDHQGFVPANYVRKLAHDEFPMLPQRRREEPENISQRQEQIENQYHSLLDRAEERRRRLLQRYNEFLLAYEAGDMLDWIREKKAENTGVELDDVWELQKKFDEFQTDLKTNEPRLRDINKVADDLLFEGLLTPEGTQIQQELNARWGSLQRLAEEQRQLLGSAHAVQMFHRDADDTKEQIEKKCQALSAADPGSDLFSVQALQRQHEGFERDLTPLGEKVNILGETANRLSESHPDATDDLQRQRLELKEAWEDLLGHTEDRKENLQEALKFYLFLSQARDLQNWISGIGGMVSSQELAEDLTGTEILIERHQEQRDEIEAEAPTFQVLEDFGRDLISSGHRASPEIEEKLQTVRLERDELEKAWEQRKKMLDQCLELQLFRVDCDQAENWMVARENYLSSDDKGSLDSLGALMKKCDDLDKAITTQDKKITELELFAERLIADDHYAQEEIAVRLQRILDRWKALKAQLIAERTKLGDSADLKQFYRDLEDLNEWISEMLPTACDESYKDTTNIQRKYLKHKTFENEVHGRTEEVEGVINLGNALVERRACDGNEETVKGQVEELEKEWNHLLERTADKGQKLNEASRQQRFNTGIRDFEFWLSEAETLLSMKDQARDLASAGNLLKKHQLLETEMLARKDALKDLDTLATDLISSGTFNTEQIVEKRDNVNKRFLNVEQLSAEHHEKLKEDYALFQFFQDLDNEEFWIEEKLVQVRSQDYGRDLHGVQNLLKKHKRLEGELVAHEPAIQNVLDMAATLGDKTTVGREAIQERLDQFVQHWEQLKELTKARGFQLGESLEYLEFMENAEEEEAWLSEQETMVAQGDSGDSLATTQSLLKKLEALENDFAAHEIQVQNVCAQGRDILSKEESQHKEEIATKIEALNEKTPSLAKAIAAWKSRLEDDHSFQQFNWKADVVETWIAEKETSLKTNGNGADLAAFLTLLAKQDTLDATLQSFQQERLSEITDLKDQLVTAEHNQTKAIEERHAALLRRWEQLLEASEAHRQKLLEKQLPLQKAEDLFMEFAHKASAFNNWCENVEEDLSEPVHCVSLDAIRQLQKDHEAFLSSLARAQSDFNYLLELDQQIKALNVPSSPYTWLTVEALERIWKHLSDIIKEREQELEKEEARQVKNFEMCQEFEQNASAFLNWILETRAYFLDGSLLKETGTLESQLEANKRKQKEIQAMKRQLTKIEDLGEKLEEALVLDIKFSTIGLAQQWDQLFQLGVRRQHNLEQQIQIRDTPGVSEETLEEFKTTYRHFDENLTGRLSHKDFRSCLRGLNYYLPMVEEGESEPKFEKFLDAVDPGRKGYVTQEDYTYFLIDKESENIKSSDEIENSFQALAEGKAYITKEDMKQALTPEQVSFCASHMQQYVDPRGRSHPAGYDYVGFINSYFGN

Entity 5 Entity 5 polymer

Description description	Actin, cytoplasmic 1
Molecular weight formula_weight	41782.7 kDa
Source method src_method	nat
Copy count entity_count	12

Polymer Polymer

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

MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF

Entity 6 Entity 6 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 7 Entity 7 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 8 Entity 8 polymer

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

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	V,W,X

MAGITTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEEHLCTQRMLDQTLLDLNEM

Entity 9 Entity 9 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 10 Entity 10 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 11 Entity 11 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	12

▼

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	8iahA01
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	8iahB01
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	8iahC01
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	8iahD01
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	8iahE01
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	8iahF01
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	8iahH01
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	8iahI01
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	8iahJ01
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	8iahK01
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	8iahL01
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	8iahY01
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily	10 — Ribonuclease Inhibitor

▶

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	3.60 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	43000

Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State I, 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

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Beta-adducin

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Dematin actin binding protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Spectrin alpha, erythrocytic 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

Spectrin beta chain

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Tropomyosin 3

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Tropomodulin-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

SH3 domain-binding glutamic acid-rich-like protein

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

8iah__assembly_1__model_1

8iah__assembly_1__model_1 | I(q)

8iah__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment