9CVC: CDAN1 dimer with three ASF1A

CDAN1 dimer with three ASF1A. Determined by electron microscopy at 3.5 Å resolution. Released 26 Mar 2025.

Method: Electron microscopy
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 5
Atoms: 12,564
Mol. weight: 361.02 kDa
Released: 26 Mar 2025

Explore 9CVC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9CVC contains 77 α-helices and 44 β-strands across 5 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 31 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	3-9	7
α-helix	15-22	8
α-helix	33-42	10
α-helix	43-45	3
α-helix	49-61	13
β-strand	196	1	1
β-strand	200	1	2
α-helix	207-209	3
α-helix	299-314	16
α-helix	321-332	12
α-helix	363-376	14
α-helix	379-382	4
α-helix	386-394	9
α-helix	396-401	6
α-helix	403-418	16
α-helix	447-468	22
α-helix	477-494	18
α-helix	498-513	16
α-helix	536-549	14
α-helix	560-562	3
α-helix	567-578	12
α-helix	581-599	19
α-helix	616-644	29
α-helix	661-667	7
α-helix	671-672	2
α-helix	676-685	10
α-helix	689-700	12
α-helix	711-725	15
α-helix	739-753	15
α-helix	760-763	4
α-helix	792-798	7
α-helix	803-817	15
β-strand	827	1	3
α-helix	828-829	2
β-strand	830	1	4

Chain B: 30 helices, 0 β-strands

Element	Residues	Length
α-helix	2-9	8
α-helix	15-22	8
α-helix	33-42	10
α-helix	43-45	3
α-helix	49-61	13
α-helix	299-314	16
α-helix	321-332	12
α-helix	363-376	14
α-helix	379-382	4
α-helix	386-394	9
α-helix	396-401	6
α-helix	403-418	16
α-helix	447-468	22
α-helix	477-494	18
α-helix	498-513	16
α-helix	536-549	14
α-helix	560-562	3
α-helix	567-578	12
α-helix	581-599	19
α-helix	616-644	29
α-helix	661-667	7
α-helix	671-672	2
α-helix	676-686	11
α-helix	689-700	12
α-helix	711-725	15
α-helix	739-753	15
α-helix	760-763	4
α-helix	783-786	4
α-helix	792-798	7
α-helix	803-817	15

Chain C: 6 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	5
β-strand	16-17	2	3
α-helix	21-22	2
β-strand	24-30	7	5
β-strand	38-44	7	3
α-helix	51-53	3
β-strand	55-62	8	3
β-strand	68-69	2	5
β-strand	71	1	4
β-strand	72-73	2	5
α-helix	77-80	4
α-helix	87-90	4
β-strand	93-101	9	3
β-strand	104-107	4	3
β-strand	110-117	8	3
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	3
β-strand	145	1	3
β-strand	148	1	3

Chain D: 4 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	2
α-helix	20-21	2
β-strand	22-30	9	2
β-strand	38-44	7	1
β-strand	55-62	8	1
β-strand	68-76	9	2
α-helix	78-80	3
α-helix	87-90	4
β-strand	93	1	6
β-strand	95-99	5	1
β-strand	100-101	2	7
β-strand	104-105	2	7
β-strand	113	1	6
β-strand	116	1	8
α-helix	120-124	5
β-strand	136	1	8
β-strand	140	1	6

Chain E: 6 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	9
β-strand	15-17	3	10
α-helix	21	1
β-strand	22	1	11
β-strand	24-30	7	9
β-strand	38-45	8	10
α-helix	51-53	3
β-strand	54-62	9	10
β-strand	68-69	2	9
β-strand	76	1	11
α-helix	77-80	4
α-helix	87-90	4
β-strand	93-101	9	10
β-strand	104-107	4	10
β-strand	110-117	8	10
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	10
β-strand	148	1	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Codanin-1	A, B	protein	1277	Homo sapiens	Q8IWY9 (AlphaFold model)
Histone chaperone ASF1A	C, D, E	protein	241	Homo sapiens	Q9Y294 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9CVC_1 Codanin-1 (chains A, B)
MASWSHPQFEKGAWSHPQFEKGSWSHPQFEKGPAGSENLYFQGSGIRDRTMAAVLESLLR
EEVSVAAVVRWIARSTQGSEDNAGEAAALSSLRALRKEFVPFLLNFLREQSSRVLPQGPP
TPAKTPGASAALPGRPGGPPRGSRGARSQLFPPTEAQSTAAEAPLARRGGRRRGPGPARE
RGGRGLEEGVSGESLPGAGGRRLRGSGSPSRPSLTLSDPPNLSNLEEFPPVGSVPPGPTG
TKPSRRINPTPVSEERSLSKPKTCFTSPPISCVPSSQPSALDTSPWGLGLPPGCRSLQEE
REMLRKERSKQLQQSPTPTCPTPELGSPLPSRTGSLTDEPADPARVSSRQRLELVALVYS
SCIAENLVPNLFLELFFVFQLLTARRMVTAKDSDPELSPAVLDSLESPLFQSIHDCVFFA
VQVLECHFQVLSNLDKGTLKLLAENERLLCFSPALQGRLRAAYEGSVAVVSLVMPPSTQA
VSFQPETDNRANFSSDRAFHTFKKQRDVFYEVLREWEDHHEEPGWDFEKGLGSRIRAMMG
QLSAACSHSHFVRLFQKQLLQMCQSPGGAGGTVLGEAPDVLSMLGADKLGRLWRLQERLM
APQSSGGPCPPPTFPGCQGFFRDFILSASSFQFNQHLMDSLSLKIQELNGLALPQHEPND
EDGESDVDWQGERKQFAVVLLSLRLLAKFLGFVAFLPYRGPEPPPTGELQDSILALRSQV
PPVLDVRTLLQRGLQARRAVLTVPWLVEFLSFADHVVPLLEYYRDIFTLLLRLHRSLVLS
QESEGKMCFLNKLLLLAVLGWLFQIPTVPEDLFFLEEGPSYAFEVDTVAPEHGLDNAPVV
DQQLLYTCCPYIGELRKLLASWVSGSSGRSGGFMRKITPTTTTSLGAQPSQTSQGLQAQL
AQAFFHNQPPSLRRTVEFVAERIGSNCVKHIKATLVADLVRQAESLLQEQLVTQGEEGGD
PAQLLEILCSQLCPHGAQALALGREFCQRKSPGAVRALLPEETPAAVLSSAENIAVGLAT
EKACAWLSANITALIRREVKAAVSRTLRAQGPEPAARGERRGCSRACEHHAPLPSHLISE
IKDVLSLAVGPRDPDEGVSPEHLEQLLGQLGQTLRCRQFLCPPAEQHLAKCSVELASLLV
ADQIPILGPPAQYRLERGQARRLLHMLLSLWKEDFQGPVPLQLLLSPRNVGLLADTRPRE
WDLLLFLLRELVEKGLMGRMEIEACLGSLHQAQWPGDFAEELATLSNLFLAEPHLPEPQL
RACELVQPNRGTVLAQS

Sequence of entity 2 (C, D, E), FASTA

>9CVC_2 Histone chaperone ASF1A (chains C, D, E)
MAVYPYDVPDYAGYPYDVPDYAGSYPYDVPDYAPAGSMAKVQVNNVVVLDNPSPFYNPFQ
FEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGL
IPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASN
PRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDC
M

Primary citation

Mechanism of ASF1 engagement by CDAN1. Sedor, S.F., Shao, S. Nat Commun (2025) 16:2599-2599. DOI 10.1038/s41467-025-57950-z · PubMed

Other PDB entries of the same protein (UniProt Q8IWY9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9IMZ 3.75 Å, CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate histone supply

Browse structure collections

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