6E2H: Human Ash2L

Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length DPY-30. Determined by X-ray diffraction at 2.24 Å resolution. Released 8 Aug 2018.

Method: X-ray diffraction
Resolution: 2.24 Å
Organism: Homo sapiens
Chains: 3
Atoms: 2,663
Mol. weight: 46.61 kDa
Released: 8 Aug 2018

Explore 6E2H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6E2H contains 11 α-helices and 17 β-strands across 3 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 D: 3 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	289-294	6	1
β-strand	299-300	2	2
β-strand	306-308	3	2
β-strand	314-318	5	1
β-strand	322	1	3
β-strand	325-335	11	2
β-strand	341-347	7	1
β-strand	363-367	5	1
β-strand	373-375	3	1
β-strand	378-380	3	1
β-strand	391-398	8	2
β-strand	409-414	6	2
β-strand	417-424	8	2
α-helix	426-428	3
β-strand	431	1	3
β-strand	432-438	7	1
β-strand	442-446	5	2
β-strand	461-462	2	2
α-helix	463-466	4
α-helix	468-488	21

Chain E: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	53-60	8
α-helix	62-75	14
α-helix	80-90	11
α-helix	92-95	4

Chain F: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	53-58	6
α-helix	62-75	14
α-helix	80-91	12
α-helix	92-94	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Set1/Ash2 histone methyltransferase complex subunit ASH2	D	protein	214	Homo sapiens	Q9UBL3 (AlphaFold model)
Protein dpy-30 homolog	E, F	protein	100	Homo sapiens	Q9C005 (AlphaFold model)

Sequence of entity 1 (D), FASTA

>6E2H_1 Set1/Ash2 histone methyltransferase complex subunit ASH2 (chains D)
ATYAMGSMRVLLALHDRAPQLKISDDRLTVVGEKGYSMVRASHGVRKGAWYFEITVDEMP
PDTAARLGWSQPLGNLQAPLGYDKFSYSWRSKKGTKFHQSIGKHYSSGYGQGDVLGFYIN
LPEDTISGRGSEIIFYKNGVNQGVAYKDIFEGVYFPAISLYKSCTVSINFGPCFKYPPKD
LTYRPMSDMGWGAVVEHTLADVLYHVETEVDGRR

Sequence of entity 2 (E, F), FASTA

>6E2H_2 Protein dpy-30 homolog (chains E, F)
GMEPEQMLEGQTQVAENPHSEYGLTDNVERIVENEKINAEKSSKQKVDLQSLPTRAYLDQ
TVVPILLQGLAVLAKERPPNPIEFLASYLLKNKAQFEDRN

Primary citation

Structural Analysis of the Ash2L/Dpy-30 Complex Reveals a Heterogeneity in H3K4 Methylation. Haddad, J.F., Yang, Y., Takahashi, Y.H. et al. Structure (2018) 26:1594. DOI 10.1016/j.str.2018.08.004 · PubMed

Other PDB entries of the same protein (UniProt Q9UBL3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5F6L 1.9 Å, The crystal structure of MLL1 (N3861I/Q3867L) in complex with RbBP5 and Ash2L
3TOJ 2.07 Å, Structure of the SPRY domain of human Ash2L
3RSN 2.1 Å, Crystal Structure of the N-terminal region of Human Ash2L
4X8N 2.1 Å, Crystal structure of Ash2L SPRY domain in complex with phosphorylated RbBP5
7W67 2.19 Å, The crystal structure of MLL1 (N3861I/Q3867L/C3882SS)-RBBP5-ASH2L in complex with…
4X8P 2.2 Å, Crystal structure of Ash2L SPRY domain in complex with RbBP5
7W6A 2.21 Å, Crystal structure of the MLL1 (N3861I/Q3867L/C3882SS)-RBBP5-ASH2L complex
4RIQ 2.23 Å, Crystal structure of DPY-30 dimerization/docking domain in complex with Ash2L…
7W6L 2.26 Å, The crystal structure of MLL3-RBBP5-ASH2L in complex with H3K4me0 peptide
5F6K 2.41 Å, Crystal structure of the MLL3-Ash2L-RbBP5 complex
3S32 2.45 Å, Crystal structure of Ash2L N-terminal domain
7W6I 2.56 Å, The crystal structure of MLL1 (N3861I/Q3867L/C3882SS)-RBBP5-ASH2L in complex with…

Browse structure collections

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