6INE: Human ASH1L-MRG15 complex

Crystal Structure of human ASH1L-MRG15 complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 20 Mar 2019.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,443
Mol. weight: 52.35 kDa
Ligands: SAM, ZN
Released: 20 Mar 2019

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

Secondary structure: helices and β-sheets

6INE contains 26 α-helices and 24 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, 20 β-strands

Element	Residues	Length	Sheet
α-helix	2029-2032	4
α-helix	2034-2039	6
α-helix	2049-2060	12
α-helix	2062-2067	6
β-strand	2070-2071	2	1
β-strand	2076-2077	2	2
β-strand	2083	1	3
α-helix	2109-2112	4
β-strand	2115	1	3
α-helix	2116-2118	3
α-helix	2125-2127	3
β-strand	2142-2147	6	4
β-strand	2151-2156	6	4
β-strand	2160	1	5
β-strand	2165-2168	4	3
β-strand	2172-2175	4	2
α-helix	2176-2185	10
β-strand	2195-2197	3	2
β-strand	2202-2205	4	2
β-strand	2209-2210	2	1
α-helix	2212-2215	4
α-helix	2216	1
β-strand	2217-2218	2	6
β-strand	2224-2231	8	3
β-strand	2234-2241	8	3
β-strand	2245	1	5
α-helix	2249	1
β-strand	2250	1	4
α-helix	2251	1
β-strand	2252-2253	2	6
β-strand	2267	1	7
β-strand	2278	1	7

Chain B: 14 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	162-164	3
α-helix	165-172	8
α-helix	173-177	5
β-strand	180-182	3	8
β-strand	189	1	9
α-helix	190-202	13
α-helix	211-232	22
α-helix	236-238	3
α-helix	239-248	10
α-helix	254-257	4
β-strand	259	1	9
α-helix	260-274	15
α-helix	281-300	20
α-helix	302-305	4
α-helix	308-310	3
β-strand	311-313	3	8
α-helix	314-315	2
α-helix	316-319	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone-lysine N-methyltransferase ASH1L	A	protein	267	Homo sapiens	Q9NR48
Mortality factor 4-like protein 1	B	protein	177	Homo sapiens	Q9UBU8 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6INE_1 Histone-lysine N-methyltransferase ASH1L (chains A)
MADPGLFPAPIHVGKYLRQKRIDFQLPYDILWQWKHNQLYKKPDVPLYKKIRSNVYVDVK
PLSGYEATTCNCKKPDDDTRKGCVDDCLNRMIFAECSPNTCPCGEQCCNQRIQRHEWVQC
LERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHSDHYCLNLDSG
MVIDSYRMGNEARFINHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFN
VEKQQLCKCGFEKCRGIIGGKSQRVNG

Sequence of entity 2 (B), FASTA

>6INE_2 Mortality factor 4-like protein 1 (chains B)
SSDPMNRVEVKVKIPEELKPWLVDDWDLITRQKQLFYLPAKKNVDSILEDYANYKKSRGN
TDNKEYAVNEVVAGIKEYFNVMLGTQLLYKFERPQYAEILADHPDAPMSQVYGAPHLLRL
FVRIGAMLAYTPLDEKSLALLLNYLHDFLKYLAKNSATLFSASDYEVAPPEYHRKAV

Ligands and cofactors

ID	Name	Formula	Copies
SAM	S-adenosylmethionine	C15 H22 N6 O5 S	1
ZN	Zinc ion	Zn	3

Water and common crystallization additives (GOL) are not listed.

Primary citation

Structural Insights into Stimulation of Ash1L's H3K36 Methyltransferase Activity through Mrg15 Binding. Hou, P., Huang, C., Liu, C.P. et al. Structure (2019) 27:837. DOI 10.1016/j.str.2019.01.015 · 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)
8VLH 2.4 Å, Crystal structure of Ash1L PHD-BAH domains
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)
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)

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