1TEY: Human histone chaperone, ASF1A

Name: PDB 1TEY: NMR structure of human histone chaperone, ASF1A
Published: 2005-04-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

NMR structure of human histone chaperone, ASF1A. Determined by solution NMR. Released 12 Apr 2005.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 1,257
Mol. weight: 17.93 kDa
Released: 12 Apr 2005

Explore 1TEY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1TEY contains 4 α-helices and 9 β-strands across 1 chain. 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: 4 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	1
β-strand	16-17	2	2
β-strand	22-30	9	1
α-helix	37	1
β-strand	38-44	7	2
α-helix	51-53	3
β-strand	55-62	8	2
β-strand	68-76	9	1
α-helix	86-89	4
β-strand	92-101	10	2
β-strand	104-117	14	2
α-helix	120-124	5
β-strand	135-148	14	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ASF1 anti-silencing function 1 homolog A	A	protein	158	Homo sapiens	Q9Y294 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1TEY_1 ASF1 anti-silencing function 1 homolog A (chains A)
GAMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLD
SVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYT
ETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDN

Primary citation

Structural basis for the interaction of Asf1 with histone H3 and its functional implications. Mousson, F., Lautrette, A., Thuret, J.Y. et al. Proc Natl Acad Sci U S A (2005) 102:5975-5980. DOI 10.1073/pnas.0500149102 · PubMed

Other PDB entries of the same protein (UniProt Q9Y294 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9SVO 1.6 Å, Crystal structure hASF1A 156-cr5
9TRB 1.65 Å, Crystal structure hASF1A 156-cr13
9SQK 1.7 Å, Crystal structure hASF1A 156-cr17
6ZUF 1.8 Å, Urea-based Foldamer Inhibitor chimera C2 in complex with ASF1 Histone chaperone
6F0H 1.98 Å, Crystal structure ASF1-ip4
9SS3 2.0 Å, Crystal structure hASF1A 156-cr7
6F0F 2.0 Å, Crystal structure ASF1-ip2_s
7LNY 2.1 Å, Apo structure of the Histone chaperone ASF1A residues 1-155
8CJ2 2.13 Å, Urea-based foldamer inhibitor c3u_5 chimera in complex with ASF1 histone chaperone
6F0G 2.3 Å, Crystal structure ASF1-ip3
8CJ1 2.56 Å, Urea-based foldamer inhibitor c3u_3 chimera in complex with ASF1 histone chaperone
2I32 2.7 Å, Structure of a human ASF1a-HIRA complex and insights into specificity of histone…

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