8VLH: Ash1L PHD-BAH domains

Crystal structure of Ash1L PHD-BAH domains. Determined by X-ray diffraction at 2.4 Å resolution. Released 19 Mar 2025.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,259
Mol. weight: 62.27 kDa
Ligands: SR, ZN
Released: 19 Mar 2025

Explore 8VLH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8VLH contains 22 α-helices and 42 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: 10 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	2586	1	1
β-strand	2599-2601	3	1
β-strand	2608-2610	3	1
β-strand	2637-2638	2	2
α-helix	2646-2647	2
β-strand	2651-2658	8	2
β-strand	2661-2664	4	2
β-strand	2668-2671	4	2
α-helix	2672-2673	2
β-strand	2674	1	3
α-helix	2682-2683	2
β-strand	2685	1	3
α-helix	2688-2690	3
α-helix	2696-2698	3
β-strand	2700-2709	10	2
β-strand	2715-2723	9	2
α-helix	2725-2727	3
β-strand	2736	1	4
β-strand	2740	1	5
β-strand	2742-2751	10	2
α-helix	2752-2754	3
β-strand	2755-2759	5	2
β-strand	2760-2762	3	5
α-helix	2764-2769	6
β-strand	2770-2772	3	6
α-helix	2777-2779	3
β-strand	2780-2782	3	5
β-strand	2785-2787	3	2
β-strand	2794-2796	3	2
α-helix	2803-2805	3
β-strand	2811-2813	3	6
β-strand	2824	1	4

Chain B: 12 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	2586	1	7
β-strand	2599-2601	3	7
β-strand	2608-2610	3	7
α-helix	2611-2614	4
β-strand	2637-2638	2	8
α-helix	2642-2643	2
α-helix	2646-2647	2
β-strand	2651-2658	8	8
β-strand	2661-2664	4	8
β-strand	2668-2671	4	8
β-strand	2675-2677	3	9
β-strand	2683-2685	3	9
α-helix	2686-2687	2
α-helix	2688-2690	3
α-helix	2696-2698	3
β-strand	2700-2709	10	8
β-strand	2715-2723	9	8
α-helix	2725-2727	3
β-strand	2740	1	10
β-strand	2742-2751	10	8
α-helix	2752-2754	3
β-strand	2755-2759	5	8
β-strand	2760-2762	3	10
α-helix	2764-2769	6
β-strand	2770-2772	3	11
α-helix	2777-2779	3
β-strand	2780-2782	3	10
β-strand	2785-2786	2	8
β-strand	2795-2796	2	8
α-helix	2803-2805	3
β-strand	2811-2813	3	11
α-helix	2814	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone-lysine N-methyltransferase ASH1L	A, B	protein	259	Homo sapiens	Q9NR48

Sequence of entity 1 (A, B), FASTA

>8VLH_1 Histone-lysine N-methyltransferase ASH1L (chains A, B)
GPLDVIRCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDVEHYLCEQCDPRPVDREVPMI
PRPHYAQPGCVYFICLLRDDLLLRQGDCVYLMRDSRRTPDGHPVRQSYRLLSHINRDKLD
IFRIEKLWKNEKEERFAFGHHYFRPHETHHSPSRRFYHNELFRVPLYEIIPLEAVVGTCC
VLDLYTYCKGRPKGVKEQDVYICDYRLDKSAHLFYKIHRNRYPVCTKPYAFDHFPKKLTP
KKDFSPHYVPDNYKRNGGR

Ligands and cofactors

ID	Name	Formula	Copies
SR	Strontium ion	Sr	1
ZN	Zinc ion	Zn	4

Primary citation

Structure-function relationship of ASH1L and histone H3K36 and H3K4 methylation. Vann, K.R., Sharma, R., Hsu, C.C. et al. Nat Commun (2025) 16:2235-2235. DOI 10.1038/s41467-025-57556-5 · PubMed

Other PDB entries of the same protein (UniProt Q9NR48), best resolution first:

8VLF 1.34 Å, Crystal structure of Ash1L PHD finger in complex with histone H3K4me3
6WZW 1.69 Å, Ash1L SET domain in complex with AS-85
6X0P 1.69 Å, Ash1L SET domain Q2265A mutant in complex with AS-5
8VLD 1.92 Å, Crystal structure of Ash1L PHD finger in complex with histone H3K4me2
4YNM 2.19 Å, ASH1L wild-type SET domain in complex with S-adenosyl methionine (SAM)
4YPE 2.2 Å, ASH1L SET domain H2193F mutant in complex with S-adenosyl methionine (SAM)
4YPA 2.3 Å, ASH1L SET domain Q2265A mutant in complex with S-adenosyl methionine (SAM)
3MQM 2.54 Å, Crystal Structure of the Bromodomain of human ASH1L
4YPU 2.6 Å, ASH1L SET domain K2264L mutant in complex with S-adenosyl methionine (SAM)
6INE 2.6 Å, Crystal Structure of human ASH1L-MRG15 complex
3OPE 2.9 Å, Structural Basis of Auto-inhibitory mechanism of Histone methyltransferase
4YNP 2.9 Å, ASH1L SET domain S2259M mutant in complex with S-adenosyl methionine (SAM)

Browse structure collections

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