2H1E: Tandem chromodomains of budding yeast CHD1

Tandem chromodomains of budding yeast CHD1. Determined by X-ray diffraction at 2.2 Å resolution. Released 27 Mar 2007.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 2,934
Mol. weight: 42.89 kDa
Released: 27 Mar 2007

Explore 2H1E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2H1E contains 26 α-helices and 12 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: 12 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	15-23	9	1
α-helix	24	1
α-helix	29-32	4
α-helix	40-46	7
β-strand	47-53	7	1
α-helix	58-60	3
β-strand	62-64	3	1
α-helix	66-69	4
α-helix	75-81	7
α-helix	82-88	7
α-helix	89-94	6
α-helix	100-119	20
β-strand	123-133	11	2
α-helix	134	1
β-strand	139-147	9	2
β-strand	156-159	4	2
α-helix	160-166	7
α-helix	168-174	7

Chain B: 14 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	15-23	9	3
α-helix	24	1
α-helix	29-32	4
α-helix	37-39	3
α-helix	40-46	7
β-strand	47-53	7	3
α-helix	58-60	3
β-strand	62-64	3	3
α-helix	66-69	4
α-helix	75-81	7
α-helix	82-88	7
α-helix	89-94	6
α-helix	100-119	20
β-strand	123-133	11	4
α-helix	134	1
β-strand	139-147	9	4
α-helix	152-154	3
β-strand	156-159	4	4
α-helix	160-166	7
α-helix	168-172	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chromo domain protein 1	A, B	protein	177	Saccharomyces cerevisiae	P32657 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2H1E_1 Chromo domain protein 1 (chains A, B)
MKKHHHHHHEDFHGIDIVINHRLKTSLEEGKVLEKTVPDLNNCKENYEFLIKWTDESHLH
NTWETYESIGQVRGLKRLDNYCKQFIIEDQQVRLDPYVTAEDIEIMDMERERRLDEFEEF
HVPERIIDSQRASLEDGTSQLQYLVKWRRLNYDEATWENATDIVKLAPEQVKHFQKK

Primary citation

Molecular Implications of Evolutionary Differences in CHD Double Chromodomains. Flanagan, J.F., Blus, B.J., Kim, D. et al. J Mol Biol (2007) 369:334-342. DOI 10.1016/j.jmb.2007.03.024 · PubMed

Other PDB entries of the same protein (UniProt P32657 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2XB0 2.0 Å, DNA-binding domain from Saccharomyces cerevisiae chromatin- remodelling protein Chd1
3TED 2.0 Å, Crystal structure of the Chd1 DNA-binding domain in complex with a DNA duplex
7TN2 2.3 Å, Composite model of a Chd1-nucleosome complex in the nucleotide-free state derived from…
9N6H 2.54 Å, 2.54 A S.cerevisiae Chd1[L886G/L889G/L891G]-nucleosome 1:1 complex
9N6I 2.61 Å, 2.61 A S.cerevisiae Chd1[L886G/L889G/L891G]-nucleosome 2:1 complex
7NKX 2.9 Å, RNA polymerase II-Spt4/5-nucleosome-Chd1 structure
9N6K 2.9 Å, 2.88 A S.cerevisiae Chd1[L886G/L889G/L891G]-nucleosome 2:1 complex with DNA-binding domain
5J70 2.96 Å, The Chd1 DNA-binding domain in complex with 17mer DNA duplex
9GD3 3.0 Å, Structure of a mononucleosome bound by one copy of Chd1 with the DBD on the exit-side DNA.
3MWY 3.7 Å, Crystal structure of the chromodomain-ATPase portion of the yeast Chd1 chromatin remodeler
9R5S 3.8 Å, Structural characterisation of chromatin remodelling intermediates supports linker DNA…
9GD1 4.0 Å, Structure of Chd1 bound to a hexasome-nucleosome complex with a dyad-to-dyad distance of…

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