1TEY: Human histone chaperone, ASF1A

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

ElementResiduesLengthSheet
β-strand4-1291
β-strand16-1722
β-strand22-3091
α-helix371
β-strand38-4472
α-helix51-533
β-strand55-6282
β-strand68-7691
α-helix86-894
β-strand92-101102
β-strand104-117142
α-helix120-1245
β-strand135-148142

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ASF1 anti-silencing function 1 homolog AAprotein158Homo sapiensQ9Y294 (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:

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