9caa

Cryo-EM structure of human SRCAP-nucleosome complex in the pre-engaged state (composite structure)

Method: ELECTRON MICROSCOPY

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

Helicase SRCAP

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 18 DNA 2	Vacuolar protein sorting-associated protein 72 homolog × 1 （Q15906） Actin-related protein 6 × 1 （Q9GZN1） Zinc finger HIT domain-containing protein 1 × 1 （O43257） RuvB-like 1 × 3 （Q9Y265） RuvB-like 2 × 3 （Q9Y230） Histone H2A type 1 × 2 （P06897） Histone H2B 1.1 × 2 （P02281） Histone H3.2 × 2 （P84233） Histone H4 × 2 （P62799） DNA (285-MER) × 1 DNA (285-MER) × 1 PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 4 ZINC ION × 2 ADENOSINE-5'-DIPHOSPHATE × 6	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SRCAP_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–3230； UniProt 1–3230

Vacuolar protein sorting-associated protein 72 homolog

OrganismNot specified

UniProt Q15906

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 18 DNA 2	Helicase SRCAP × 1 （Q6ZRS2） Actin-related protein 6 × 1 （Q9GZN1） Zinc finger HIT domain-containing protein 1 × 1 （O43257） RuvB-like 1 × 3 （Q9Y265） RuvB-like 2 × 3 （Q9Y230） Histone H2A type 1 × 2 （P06897） Histone H2B 1.1 × 2 （P02281） Histone H3.2 × 2 （P84233） Histone H4 × 2 （P62799） DNA (285-MER) × 1 DNA (285-MER) × 1 PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 4 ZINC ION × 2 ADENOSINE-5'-DIPHOSPHATE × 6	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VPS72_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–364； UniProt 1–364

Actin-related protein 6

OrganismNot specified

UniProt Q9GZN1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 18 DNA 2	Helicase SRCAP × 1 （Q6ZRS2） Vacuolar protein sorting-associated protein 72 homolog × 1 （Q15906） Zinc finger HIT domain-containing protein 1 × 1 （O43257） RuvB-like 1 × 3 （Q9Y265） RuvB-like 2 × 3 （Q9Y230） Histone H2A type 1 × 2 （P06897） Histone H2B 1.1 × 2 （P02281） Histone H3.2 × 2 （P84233） Histone H4 × 2 （P62799） DNA (285-MER) × 1 DNA (285-MER) × 1 PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 4 ZINC ION × 2 ADENOSINE-5'-DIPHOSPHATE × 6	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ARP6_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–396； UniProt 1–396

Zinc finger HIT domain-containing protein 1

OrganismNot specified

UniProt O43257

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 18 DNA 2	Helicase SRCAP × 1 （Q6ZRS2） Vacuolar protein sorting-associated protein 72 homolog × 1 （Q15906） Actin-related protein 6 × 1 （Q9GZN1） RuvB-like 1 × 3 （Q9Y265） RuvB-like 2 × 3 （Q9Y230） Histone H2A type 1 × 2 （P06897） Histone H2B 1.1 × 2 （P02281） Histone H3.2 × 2 （P84233） Histone H4 × 2 （P62799） DNA (285-MER) × 1 DNA (285-MER) × 1 PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 4 ZINC ION × 2 ADENOSINE-5'-DIPHOSPHATE × 6	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ZNHI1_HUMAN
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain D； PDBConstruct 1–154； UniProt 1–154

RuvB-like 1

OrganismNot specified

UniProt Q9Y265

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 18 DNA 2	Helicase SRCAP × 1 （Q6ZRS2） Vacuolar protein sorting-associated protein 72 homolog × 1 （Q15906） Actin-related protein 6 × 1 （Q9GZN1） Zinc finger HIT domain-containing protein 1 × 1 （O43257） RuvB-like 2 × 3 （Q9Y230） Histone H2A type 1 × 2 （P06897） Histone H2B 1.1 × 2 （P02281） Histone H3.2 × 2 （P84233） Histone H4 × 2 （P62799） DNA (285-MER) × 1 DNA (285-MER) × 1 PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 4 ZINC ION × 2 ADENOSINE-5'-DIPHOSPHATE × 6	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RUVB1_HUMAN
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain E； PDBConstruct 1–456； UniProt 1–456 Author chain G； PDBConstruct 1–456； UniProt 1–456 Author chain I； PDBConstruct 1–456； UniProt 1–456

RuvB-like 2

OrganismNot specified

UniProt Q9Y230

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 18 DNA 2	Helicase SRCAP × 1 （Q6ZRS2） Vacuolar protein sorting-associated protein 72 homolog × 1 （Q15906） Actin-related protein 6 × 1 （Q9GZN1） Zinc finger HIT domain-containing protein 1 × 1 （O43257） RuvB-like 1 × 3 （Q9Y265） Histone H2A type 1 × 2 （P06897） Histone H2B 1.1 × 2 （P02281） Histone H3.2 × 2 （P84233） Histone H4 × 2 （P62799） DNA (285-MER) × 1 DNA (285-MER) × 1 PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 4 ZINC ION × 2 ADENOSINE-5'-DIPHOSPHATE × 6	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RUVB2_HUMAN
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain F； PDBConstruct 1–463； UniProt 1–463 Author chain H； PDBConstruct 1–463； UniProt 1–463 Author chain J； PDBConstruct 1–463； UniProt 1–463

Histone H2A type 1

Xenopus laevis

UniProt P06897

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 18 DNA 2	Helicase SRCAP × 1 （Q6ZRS2） Vacuolar protein sorting-associated protein 72 homolog × 1 （Q15906） Actin-related protein 6 × 1 （Q9GZN1） Zinc finger HIT domain-containing protein 1 × 1 （O43257） RuvB-like 1 × 3 （Q9Y265） RuvB-like 2 × 3 （Q9Y230） Histone H2B 1.1 × 2 （P02281） Histone H3.2 × 2 （P84233） Histone H4 × 2 （P62799） DNA (285-MER) × 1 DNA (285-MER) × 1 PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 4 ZINC ION × 2 ADENOSINE-5'-DIPHOSPHATE × 6	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	H2A1_XENLA
Isoform	—
PDB entities	7
Chains and sequence ranges	Author chain Q； PDBConstruct 1–122； UniProt 2–123 Author chain S； PDBConstruct 1–122； UniProt 2–123

Histone H2B 1.1

Xenopus laevis

UniProt P02281

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 18 DNA 2	Helicase SRCAP × 1 （Q6ZRS2） Vacuolar protein sorting-associated protein 72 homolog × 1 （Q15906） Actin-related protein 6 × 1 （Q9GZN1） Zinc finger HIT domain-containing protein 1 × 1 （O43257） RuvB-like 1 × 3 （Q9Y265） RuvB-like 2 × 3 （Q9Y230） Histone H2A type 1 × 2 （P06897） Histone H3.2 × 2 （P84233） Histone H4 × 2 （P62799） DNA (285-MER) × 1 DNA (285-MER) × 1 PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 4 ZINC ION × 2 ADENOSINE-5'-DIPHOSPHATE × 6	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	H2B11_XENLA
Isoform	—
PDB entities	8
Chains and sequence ranges	Author chain R； PDBConstruct 1–125； UniProt 2–126 Author chain T； PDBConstruct 1–125； UniProt 2–126

Histone H3.2

Xenopus laevis

UniProt P84233

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 18 DNA 2	Helicase SRCAP × 1 （Q6ZRS2） Vacuolar protein sorting-associated protein 72 homolog × 1 （Q15906） Actin-related protein 6 × 1 （Q9GZN1） Zinc finger HIT domain-containing protein 1 × 1 （O43257） RuvB-like 1 × 3 （Q9Y265） RuvB-like 2 × 3 （Q9Y230） Histone H2A type 1 × 2 （P06897） Histone H2B 1.1 × 2 （P02281） Histone H4 × 2 （P62799） DNA (285-MER) × 1 DNA (285-MER) × 1 PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 4 ZINC ION × 2 ADENOSINE-5'-DIPHOSPHATE × 6	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	H32_XENLA
Isoform	—
PDB entities	9
Chains and sequence ranges	Author chain U； PDBConstruct 1–135； UniProt 2–136 Author chain W； PDBConstruct 1–135； UniProt 2–136

Histone H4

Xenopus laevis

UniProt P62799

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–DNA	Heteromer	Protein 18 DNA 2	Helicase SRCAP × 1 （Q6ZRS2） Vacuolar protein sorting-associated protein 72 homolog × 1 （Q15906） Actin-related protein 6 × 1 （Q9GZN1） Zinc finger HIT domain-containing protein 1 × 1 （O43257） RuvB-like 1 × 3 （Q9Y265） RuvB-like 2 × 3 （Q9Y230） Histone H2A type 1 × 2 （P06897） Histone H2B 1.1 × 2 （P02281） Histone H3.2 × 2 （P84233） DNA (285-MER) × 1 DNA (285-MER) × 1 PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MAGNESIUM ION × 4 ZINC ION × 2 ADENOSINE-5'-DIPHOSPHATE × 6	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	H4_XENLA
Isoform	—
PDB entities	10
Chains and sequence ranges	Author chain V； PDBConstruct 1–102； UniProt 2–103 Author chain X； PDBConstruct 1–102； UniProt 2–103

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	9caa
Deposition date deposition_date	2024-06-17
Structure title title	Cryo-EM structure of human SRCAP-nucleosome complex in the pre-engaged state (composite structure)
Keywords keywords	Chromatin Remodeler, Snf2 family ATPase, H2A.Z, GENE REGULATION; GENE REGULATION
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.

9caa__assembly_1__model_1

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

Download this curve (.dat)

9caa__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9caa__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	65.96 Å
Rg (electron density)	64.41 Å
Total Rg	64.73 Å
Atom count	40983
Residues	4692
Excluded volume	711640 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9caa__assembly_1__model_1`	20-meric （20）	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 (16)

Entity 1 Entity 1 polymer

Description description	Helicase SRCAP
Molecular weight formula_weight	343915.2 kDa
EC 编号 ec_number	3.6.4.-
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	40983

MQSSPSPAHPQLPVLQTQMVSDGMTGSNPVSPASSSSPASSGAGGISPQHIAQDSSLDGPPGPPDGATVPLEGFSLSQAADLANKGPKWEKSHAEIAEQAKHEAEIETRIAELRKEGFWSLKRLPKVPEPPRPKGHWDYLCEEMQWLSADFAQERRWKRGVARKVVRMVIRHHEEQRQKEERARREEQAKLRRIASTMAKDVRQFWSNVEKVVQFKQQSRLEEKRKKALDLHLDFIVGQTEKYSDLLSQSLNQPLTSSKAGSSPCLGSSSAASSPPPPASRLDDEDGDFQPQEDEEEDDEETIEVEEQQEGNDAEAQRREIELLRREGELPLEELLRSLPPQLLEGPSSPSQTPSSHDSDTRDGPEEGAEEEPPQVLEIKPPPSAVTQRNKQPWHPDEDDEEFTANEEEAEDEEDTIAAEEQLEGEVDHAMELSELAREGELSMEELLQQYAGAYAPGSGSSEDEDEDEVDANSSDCEPEGPVEAEEPPQEDSSSQSDSVEDRSEDEEDEHSEEEETSGSSASEESESEESEDAQSQSQADEEEEDDDFGVEYLLARDEEQSEADAGSGPPTPGPTTLGPKKEITDIAAAAESLQPKGYTLATTQVKTPIPLLLRGQLREYQHIGLDWLVTMYEKKLNGILADEMGLGKTIQTISLLAHLACEKGNWGPHLIIVPTSVMLNWEMELKRWCPSFKILTYYGAQKERKLKRQGWTKPNAFHVCITSYKLVLQDHQAFRRKNWRYLILDEAQNIKNFKSQRWQSLLNFNSQRRLLLTGTPLQNSLMELWSLMHFLMPHVFQSHREFKEWFSNPLTGMIEGSQEYNEGLVKRLHKVLRPFLLRRVKVDVEKQMPKKYEHVIRCRLSKRQRCLYDDFMAQTTTKETLATGHFMSVINILMQLRKVCNHPNLFDPRPVTSPFITPGICFSTASLVLRATDVHPLQRIDMGRFDLIGLEGRVSRYEADTFLPRHRLSRRVLLEVATAPDPPPRPKPVKMKVNRMLQPVPKQEGRTVVVVNNPRAPLGPVPVRPPPGPELSAQPTPGPVPQVLPASLMVSASPAGPPLIPASRPPGPVLLPPLQPNSGSLPQVLPSPLGVLSGTSRPPTPTLSLKPTPPAPVRLSPAPPPGSSSLLKPLTVPPGYTFPPAAATTTSTTTATATTTAVPAPTPAPQRLILSPDMQARLPSGEVVSIGQLASLAQRPVANAGGSKPLTFQIQGNKLTLTGAQVRQLAVGQPRPLQRNVVHLVSAGGQHHLISQPAHVALIQAVAPTPGPTPVSVLPSSTPSTTPAPTGLSLPLAANQVPPTMVNNTGVVKIVVRQAPRDGLTPVPPLAPAPRPPSSGLPAVLNPRPTLTPGRLPTPTLGTARAPMPTPTLVRPLLKLVHSPSPEVSASAPGAAPLTISSPLHVPSSLPGPASSPMPIPNSSPLASPVSSTVSVPLSSSLPISVPTTLPAPASAPLTIPISAPLTVSASGPALLTSVTPPLAPVVPAAPGPPSLAPSGASPSASALTLGLATAPSLSSSQTPGHPLLLAPTSSHVPGLNSTVAPACSPVLVPASALASPFPSAPNPAPAQASLLAPASSASQALATPLAPMAAPQTAILAPSPAPPLAPLPVLAPSPGAAPVLASSQTPVPVMAPSSTPGTSLASASPVPAPTPVLAPSSTQTMLPAPVPSPLPSPASTQTLALAPALAPTLGGSSPSQTLSLGTGNPQGPFPTQTLSLTPASSLVPTPAQTLSLAPGPPLGPTQTLSLAPAPPLAPASPVGPAPAHTLTLAPASSSASLLAPASVQTLTLSPAPVPTLGPAAAQTLALAPASTQSPASQASSLVVSASGAAPLPVTMVSRLPVSKDEPDTLTLRSGPPSPPSTATSFGGPRPRRQPPPPPRSPFYLDSLEEKRKRQRSERLERIFQLSEAHGALAPVYGTEVLDFCTLPQPVASPIGPRSPGPSHPTFWTYTEAAHRAVLFPQQRLDQLSEIIERFIFVMPPVEAPPPSLHACHPPPWLAPRQAAFQEQLASELWPRARPLHRIVCNMRTQFPDLRLIQYDCGKLQTLAVLLRQLKAEGHRVLIFTQMTRMLDVLEQFLTYHGHLYLRLDGSTRVEQRQALMERFNADKRIFCFILSTRSGGVGVNLTGADTVVFYDSDWNPTMDAQAQDRCHRIGQTRDVHIYRLISERTVEENILKKANQKRMLGDMAIEGGNFTTAYFKQQTIRELFDMPLEEPSSSSVPSAPEEEEETVASKQTHILEQALCRAEDEEDIRAATQAKAEQVAELAEFNENDGFPAGEGEEAGRPGAEDEEMSRAEQEIAALVEQLTPIERYAMKFLEASLEEVSREELKQAEEQVEAARKDLDQAKEEVFRLPQEEEEGPGAGDESSCGTGGGTHRRSKKAKAPERPGTRVSERLRGARAETQGANHTPVISAHQTRSTTTPPRCSPARERVPRPAPRPRPTPASAPAAIPALVPVPVSAPVPISAPNPITILPVHILPSPPPPSQIPPCSSPACTPPPACTPPPAHTPPPAQTCLVTPSSPLLLGPPSVPISASVTNLPLGLRPEAELCAQALASPESLELASVASSETSSLSLVPPKDLLPVAVEILPVSEKNLSLTPSAPSLTLEAGSIPNGQEQEAPDSAEGTTLTVLPEGEELPLCVSESNGLELPPSAASDEPLQEPLEADRTSEELTEAKTPTSSPEKPQELVTAEVAAPSTSSSATSSPEGPSPARPPRRRTSADVEIRGQGTGRPGQPPGPKVLRKLPGRLVTVVEEKELVRRRRQQRGAASTLVPGVSETSASPGSPSVRSMSGPESSPPIGGPCEAAPSSSLPTPPQQPFIARRHIELGVTGGGSPENGDGALLAITPPAVKRRRGRPPKKNRSPADAGRGVDEAPSSTLKGKTNGADPVPGPETLIVADPVLEPQLIPGPQPLGPQPVHRPNPLLSPVEKRRRGRPPKARDLPIPGTISSAGDGNSESRTQPPPHPSPLTPLPPLLVCPTATVANTVTTVTISTSPPKRKRGRPPKNPPSPRPSQLPVLDRDSTSVLESCGLGRRRQPQGQGESEGSSSDEDGSRPLTRLARLRLEAEGMRGRKSGGSMVVAVIQDDLDLADSGPGGLELTPPVVSLTPKLRSTRLRPGSLVPPLETEKLPRKRAGAPVGGSPGLAKRGRLQPPSPLGPEGSVEESEAEASGEEEEGDGTPRRRPGPRRLVGTTNQGDQRILRSSAPPSLAGPAVSHRGRKAKT

Entity 2 Entity 2 polymer

Description description	Vacuolar protein sorting-associated protein 72 homolog
Molecular weight formula_weight	40658.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MSLAGGRAPRKTAGNRLSGLLEAEEEDEFYQTTYGGFTEESGDDEYQGDQSDTEDEVDSDFDIDEGDEPSSDGEAEEPRRKRRVVTKAYKEPLKSLRPRKVNTPAGSSQKAREEKALLPLELQDDGSDSRKSMRQSTAEHTRQTFLRVQERQGQSRRRKGPHCERPLTQEELLREAKITEELNLRSLETYERLEADKKKQVHKKRKCPGPIITYHSVTVPLVGEPGPKEENVDIEGLDPAPSVSALTPHAGTGPVNPPARCSRTFITFSDDATFEEWFPQGRPPKVPVREVCPVTHRPALYRDPVTDIPYATARAFKIIREAYKKYITAHGLPPTASALGPGPPPPEPLPGSGPRALRQKIVIK

Entity 3 Entity 3 polymer

Description description	Actin-related protein 6
Molecular weight formula_weight	45857.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

MTTLVLDNGAYNAKIGYSHENVSVIPNCQFRSKTARLKTFTANQIDEIKDPSGLFYILPFQKGYLVNWDVQRQVWDYLFGKEMYQVDFLDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGALSAHRYFRDNPSELCCIIVDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQLHVMDETHVINQVKEDVCYVSQDFYRDMDIAKLKGEENTVMIDYVLPDFSTIKKGFCKPREEMVLSGKYKSGEQILRLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEEMQPHFFKNIVLTGGNSLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYAWEGGKLISENDDFEDMVVTREDYEENGHSVCEEKFDI

Entity 4 Entity 4 polymer

Description description	Zinc finger HIT domain-containing protein 1
Molecular weight formula_weight	17567.0 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

MVEKKTSVRSQDPGQRRVLDRAARQRRINRQLEALENDNFQDDPHAGLPQLGKRLPQFDDDADTGKKKKKTRGDHFKLRFRKNFQALLEEQNLSVAEGPNYLTACAGPPSRPQRPFCAVCGFPSPYTCVSCGARYCTVRCLGTHQETRCLKWTV

Entity 5 Entity 5 polymer

Description description	RuvB-like 1
Molecular weight formula_weight	50296.9 kDa
EC 编号 ec_number	3.6.4.12
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,G,I

MKIEEVKSTTKTQRIASHSHVKGLGLDESGLAKQAASGLVGQENAREACGVIVELIKSKKMAGRAVLLAGPPGTGKTALALAIAQELGSKVPFCPMVGSEVYSTEIKKTEVLMENFRRAIGLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIGLKTAKGTKQLKLDPSIFESLQKERVEAGDVIYIEANSGAVKRQGRCDTYATEFDLEAEEYVPLPKGDVHKKKEIIQDVTLHDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEINKVVNKYIDQGIAELVPGVLFVDEVHMLDIECFTYLHRALESSIAPIVIFASNRGNCVIRGTEDITSPHGIPLDLLDRVMIIRTMLYTPQEMKQIIKIRAQTEGINISEEALNHLGEIGTKTTLRYSVQLLTPANLLAKINGKDSIEKEHVEEISELFYDAKSSAKILADQQDKYMK

Entity 6 Entity 6 polymer

Description description	RuvB-like 2
Molecular weight formula_weight	51222.5 kDa
EC 编号 ec_number	3.6.4.12
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,H,J

MATVTATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQASQGMVGQLAARRAAGVVLEMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTAIAGSEIFSLEMSKTEALTQAFRRSIGVRIKEETEIIEGEVVEIQIDRPATGTGSKVGKLTLKTTEMETIYDLGTKMIESLTKDKVQAGDVITIDKATGKISKLGRSFTRARDYDAMGSQTKFVQCPDGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDEVHMLDIESFSFLNRALESDMAPVLIMATNRGITRIRGTSYQSPHGIPIDLLDRLLIVSTTPYSEKDTKQILRIRCEEEDVEMSEDAYTVLTRIGLETSLRYAIQLITAASLVCRKRKGTEVQVDDIKRVYSLFLDESRSTQYMKEYQDAFLFNELKGETMDTS

Entity 7 Entity 7 polymer

Description description	Histone H2A type 1
Molecular weight formula_weight	13907.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKTESSKSKSK

Source Source

Source organism organism	Xenopus laevis
Common name common_name	African clawed frog
NCBI taxonomy ID ncbi_taxonomy_id	8355
Host organism host_organism	Escherichia coli

Entity 8 Entity 8 polymer

Description description	Histone H2B 1.1
Molecular weight formula_weight	13848.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

PEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK

Source Source

Source organism organism	Xenopus laevis
Common name common_name	African clawed frog
NCBI taxonomy ID ncbi_taxonomy_id	8355
Host organism host_organism	Escherichia coli

Entity 9 Entity 9 polymer

Description description	Histone H3.2
Molecular weight formula_weight	15303.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	U,W

ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA

Source Source

Source organism organism	Xenopus laevis
Common name common_name	African clawed frog
NCBI taxonomy ID ncbi_taxonomy_id	8355
Host organism host_organism	Escherichia coli

Entity 10 Entity 10 polymer

Description description	Histone H4
Molecular weight formula_weight	11263.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Source Source

Source organism organism	Xenopus laevis
Common name common_name	African clawed frog
NCBI taxonomy ID ncbi_taxonomy_id	8355
Host organism host_organism	Escherichia coli

Entity 11 Entity 11 polymer

Description description	DNA (285-MER)
Molecular weight formula_weight	87851.7 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	Y

ATCGAAGGGCGCCTATATAAGGGGGTGGGGGCGCGTTCGTCCTCCCTCTCCTCGCGGCGCGAGTTTCAGGCAGCGCTGCGTCCTGCTGCGCACGTGGGAAGCCCTGCTGGAGAATCCCGGTGCGCAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCAGCTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCAGCTGTCAGATATGTACATCCTGTGATCCCCGGGTACCGAGCTCGAATTCACTGGC

Entity 12 Entity 12 polymer

Description description	DNA (285-MER)
Molecular weight formula_weight	88190.9 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	Z

GCCAGTGAATTCGAGCTCGGTACCCGGGGATCACAGGATGTACATATCTGACAGCTGCCTGGAGACTAGGGAGTAATCCCCTTGGCGGTTAAAACGCGGGGGACAGCGCGTAGCTGCGTTTAAGCGGTGCTAGAGCTGTCTACGACCAATTGAGCGGCCTGCGCACCGGGATTCTCCAGCAGGGCTTCCCACGTGCGCAGCAGGACGCAGCGCTGCCTGAAACTCGCGCCGCGAGGAGAGGGAGGACGAACGCGCCCCCACCCCCTTATATAGGCGCCCTTCGAT

Entity 13 Entity 13 non-polymer

Description description	PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
Molecular weight formula_weight	523.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 14 Entity 14 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 15 Entity 15 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 16 Entity 16 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	6

▶

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	triclinic

Resolution resolution	4.04 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	28381

Cryo-EM structure of human SRCAP-nucleosome complex in the pre-engaged state (composite structure)

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

Helicase SRCAP

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Vacuolar protein sorting-associated protein 72 homolog

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Actin-related protein 6

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Zinc finger HIT domain-containing protein 1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

RuvB-like 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

RuvB-like 2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Histone H2A type 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

Histone H2B 1.1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Histone H3.2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Histone H4

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer