4ZBJ: UBN1 peptide

UBN1 peptide bound to H3.3/H4/Asf1. Determined by X-ray diffraction at 2.25 Å resolution. Released 15 Jul 2015.

Method: X-ray diffraction
Resolution: 2.25 Å
Organisms: Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Xenopus laevis, Homo sapiens
Chains: 4
Atoms: 2,866
Mol. weight: 41.56 kDa
Released: 15 Jul 2015

Explore 4ZBJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ZBJ contains 15 α-helices and 14 β-strands across 4 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: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	1
β-strand	16-17	2	2
α-helix	21	1
β-strand	22-30	9	1
β-strand	38-45	8	2
β-strand	54-62	9	2
α-helix	65-66	2
β-strand	68-76	9	1
α-helix	77-80	4
α-helix	81-83	3
α-helix	86-89	4
β-strand	93-101	9	2
β-strand	104-117	14	2
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	2
β-strand	145-148	4	2

Chain B: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	64-78	15
β-strand	83-84	2	3
α-helix	86-113	28
α-helix	121-130	10

Chain C: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	25-28	4
α-helix	31-40	10
α-helix	48-75	28
β-strand	80-81	2	3
α-helix	83-90	8
β-strand	95-98	4	2

Chain D: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	123-127	5
β-strand	139	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone chaperone ASF1	A	protein	175	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P32447 (AlphaFold model)
Histone H3	B	protein	77	Xenopus laevis	Q6PI79 (AlphaFold model)
Histone H4	C	protein	84	Xenopus laevis	P62799 (AlphaFold model)
Ubinuclein-1	D	protein	28	Homo sapiens	Q9NPG3 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4ZBJ_1 Histone chaperone ASF1 (chains A)
PLGSPNSSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHD
QELDSILVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVN
NEYDEEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEGDLYPPEQPGV

Sequence of entity 2 (B), FASTA

>4ZBJ_2 Histone H3 (chains B)
MALIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVALFEDTNLCAIHAKRVT
IMPKDIQLARRIRGERA

Sequence of entity 3 (C), FASTA

>4ZBJ_3 Histone H4 (chains C)
MKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKR
KTVTAMDVVYALKRQGRTLYGFGG

Sequence of entity 4 (D), FASTA

>4ZBJ_4 Ubinuclein-1 (chains D)
XIQDLIDMGYGYDESDSFIDNSEAYDEL

Primary citation

Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex. Daniel Ricketts, M., Frederick, B., Hoff, H. et al. Nat Commun (2015) 6:7711-7711. DOI 10.1038/ncomms8711 · PubMed

Other PDB entries of the same protein (UniProt P32447 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1ROC 1.5 Å, Crystal structure of the histone deposition protein Asf1
5UCB 1.52 Å, Structure of antigen-Fab complex with engineered switch residue region.
2HUE 1.7 Å, Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
5UEK 1.7 Å, Structure of antigen-Fab 12E complex with Histone chaperone ASF1
5UEA 1.7 Å, Structure of antigen-Fab complex with Histone chaperone ASF1
6AYZ 2.1 Å, Crystal structure of Asf1-Fab 12E complex
2IDC 2.2 Å, Structure of the Histone H3-Asf1 Chaperone Interaction
4EO5 2.35 Å, Yeast Asf1 bound to H3/H4G94P mutant
5EII 2.44 Å, Structural determination of an protein complex of a Fab with increased solubility
6AZ2 2.48 Å, Crystal structure of Asf1-Fab 12E complex
4RRP 2.79 Å, Crystal Structure of the Fab complexed with antigen Asf1p, Northeast Structural Genomics…
9AWE 2.8 Å, The crystal structure of an engineered Protein GF with Human Kappa Fab

Browse structure collections

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