6F0Y: Rtt109 peptide

Rtt109 peptide bound to Asf1. Determined by solution NMR. Released 27 Dec 2017.

Method: Solution NMR
Organisms: Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Saccharomyces cerevisiae S288c
Chains: 2
Atoms: 1,481
Mol. weight: 21.01 kDa
Released: 27 Dec 2017

Explore 6F0Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6F0Y contains 6 α-helices and 11 β-strands across 2 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: 6 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	55-62	8	2
β-strand	68-76	9	1
α-helix	77-80	4
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
α-helix	156-158	3

Chain B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	427	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone chaperone ASF1	A	protein	172	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P32447 (AlphaFold model)
histone acetyltransferase Rtt109 C-terminus	B	protein	15	Saccharomyces cerevisiae S288c	Q07794 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6F0Y_1 Histone chaperone ASF1 (chains A)
GAMGSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQEL
DSILVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEY
DEEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEGDLYPPEQPGV

Sequence of entity 2 (B), FASTA

>6F0Y_2 histone acetyltransferase Rtt109 C-terminus (chains B)
LAITMLKPRKKAKAL

Primary citation

Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation. Lercher, L., Danilenko, N., Kirkpatrick, J. et al. Nucleic Acids Res (2018) 46:2279-2289. DOI 10.1093/nar/gkx1283 · 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
4ZBJ 2.25 Å, UBN1 peptide bound to H3.3/H4/Asf1
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…

Browse structure collections

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