9Y3D image
Deposition Date 2025-09-02
Release Date 2026-08-12
Last Version Date 2026-08-12
Entry Detail
PDB ID:
9Y3D
Title:
Extended cryo-EM structure of the human SRCAP-nucleosome complex in the fully-engaged state, with H4-bound GAS41
Biological Source:
Source Organism(s):
Xenopus laevis (Taxon ID: 8355)
synthetic construct (Taxon ID: 32630)
Homo sapiens (Taxon ID: 9606)
Expression System(s):
Method Details:
Experimental Method:
Resolution:
7.10 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Polymer Type:polypeptide(L)
Molecule:Helicase SRCAP
Chain IDs:A
Chain Length:3230
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Vacuolar protein sorting-asso
Chain IDs:B
Chain Length:364
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Actin-related protein 6
Chain IDs:C
Chain Length:396
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Zinc finger HIT domain-contai
Chain IDs:D
Chain Length:154
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:RuvB-like 1
Chain IDs:E, G, I
Chain Length:456
Number of Molecules:3
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:RuvB-like 2
Chain IDs:F, H, J
Chain Length:463
Number of Molecules:3
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Actin-like protein 6A
Chain IDs:K, M
Chain Length:429
Number of Molecules:2
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Actin, cytoplasmic 1
Chain IDs:L
Chain Length:375
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:DNA methyltransferase 1-assoc
Chain IDs:N
Chain Length:467
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:YEATS domain-containing prote
Chain IDs:O
Chain Length:227
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:Histone H2A type 1
Chain IDs:P (auth: Q), R (auth: S)
Chain Length:128
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polypeptide(L)
Molecule:Histone H2B 1.1
Chain IDs:Q (auth: R), S (auth: T)
Chain Length:125
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polypeptide(L)
Molecule:Histone H3.2
Chain IDs:T (auth: U), V (auth: W)
Chain Length:135
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polypeptide(L)
Molecule:Histone H4
Chain IDs:U (auth: V), W (auth: X)
Chain Length:102
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polydeoxyribonucleotide
Molecule:DNA (285-MER)
Chain IDs:X (auth: Y)
Chain Length:285
Number of Molecules:1
Biological Source:synthetic construct
Polymer Type:polydeoxyribonucleotide
Molecule:DNA (285-MER)
Chain IDs:Y (auth: Z)
Chain Length:285
Number of Molecules:1
Biological Source:synthetic construct
Primary Citation
Structural mechanism of histone H2A.Z exchange by human SRCAP-CFDP1 holoenzyme.
Sci Adv 12 eaei7728 eaei7728 (2026)
PMID: 42536744 DOI: 10.1126/sciadv.aei7728
Primary Citation of related structures
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