4YPA: ASH1L SET domain Q2265A mutant

Name: PDB 4YPA: ASH1L SET domain Q2265A mutant in complex with S-adenosyl methionine (SAM)
Published: 2015-09-02
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

ASH1L SET domain Q2265A mutant in complex with S-adenosyl methionine (SAM). Determined by X-ray diffraction at 2.3 Å resolution. Released 2 Sept 2015.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,254
Mol. weight: 106.22 kDa
Ligands: SAM, ZN
Released: 2 Sept 2015

Explore 4YPA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4YPA contains 44 α-helices and 90 β-strands across 4 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, 23 β-strands

Element	Residues	Length	Sheet
α-helix	2064-2068	5
β-strand	2070-2071	2	1
β-strand	2076-2077	2	2
β-strand	2083	1	3
α-helix	2093-2095	3
β-strand	2103	1	4
α-helix	2109-2112	4
β-strand	2115	1	3
α-helix	2116-2118	3
α-helix	2125-2127	3
β-strand	2128	1	4
β-strand	2142-2146	5	5
β-strand	2152-2156	5	5
β-strand	2160	1	6
β-strand	2165-2168	4	3
β-strand	2172-2175	4	2
α-helix	2176-2185	10
β-strand	2195-2199	5	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	7
β-strand	2224-2231	8	3
β-strand	2234-2241	8	3
β-strand	2245	1	6
α-helix	2249	1
β-strand	2250	1	5
α-helix	2251	1
β-strand	2252-2253	2	7
α-helix	2255-2258	4
β-strand	2259	1	2
α-helix	2260-2261	2
β-strand	2266-2267	2	8
β-strand	2278-2279	2	8

Chain B: 11 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	2070-2071	2	9
α-helix	2075	1
β-strand	2076-2077	2	10
β-strand	2083	1	11
α-helix	2087-2088	2
β-strand	2103	1	12
α-helix	2111-2113	3
β-strand	2115	1	11
α-helix	2116-2118	3
α-helix	2125-2127	3
β-strand	2128	1	12
β-strand	2142-2146	5	13
β-strand	2152-2156	5	13
β-strand	2160	1	14
β-strand	2165-2168	4	11
β-strand	2172-2175	4	10
α-helix	2178-2185	8
β-strand	2195-2197	3	10
β-strand	2202-2205	4	10
β-strand	2209-2210	2	9
α-helix	2212-2215	4
α-helix	2216	1
β-strand	2217-2218	2	15
β-strand	2224-2231	8	11
β-strand	2234-2241	8	11
β-strand	2245	1	14
α-helix	2249	1
β-strand	2250	1	13
α-helix	2251	1
β-strand	2252-2253	2	15
α-helix	2255-2257	3
β-strand	2266-2267	2	16
β-strand	2278-2279	2	16

Chain C: 11 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	2064-2068	5
β-strand	2070-2071	2	17
β-strand	2076-2077	2	18
β-strand	2083	1	19
β-strand	2103	1	20
α-helix	2111-2113	3
β-strand	2115	1	19
α-helix	2116-2118	3
α-helix	2125-2127	3
β-strand	2128	1	20
β-strand	2142-2146	5	21
β-strand	2152-2156	5	21
β-strand	2160	1	22
β-strand	2165-2168	4	19
β-strand	2172-2175	4	18
α-helix	2176-2185	10
β-strand	2195-2199	5	18
β-strand	2202-2205	4	18
β-strand	2209-2210	2	17
α-helix	2212-2215	4
α-helix	2216	1
β-strand	2217-2218	2	23
β-strand	2224-2231	8	19
β-strand	2234-2241	8	19
β-strand	2245	1	22
α-helix	2249	1
β-strand	2250	1	21
α-helix	2251	1
β-strand	2252-2253	2	23
α-helix	2255-2258	4
β-strand	2259	1	18
α-helix	2260-2261	2
β-strand	2267	1	24
β-strand	2278	1	24

Chain D: 10 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	2070-2071	2	25
β-strand	2076-2077	2	26
β-strand	2083	1	27
α-helix	2087-2088	2
β-strand	2103	1	28
α-helix	2111-2113	3
β-strand	2115	1	27
α-helix	2116-2118	3
α-helix	2125-2127	3
β-strand	2128	1	28
β-strand	2142-2146	5	29
β-strand	2152-2156	5	29
β-strand	2160	1	30
β-strand	2165-2168	4	27
β-strand	2172-2175	4	26
α-helix	2178-2185	8
β-strand	2195-2197	3	26
β-strand	2202-2205	4	26
β-strand	2209-2210	2	25
α-helix	2212-2215	4
α-helix	2216	1
β-strand	2217-2218	2	31
β-strand	2224-2231	8	27
β-strand	2234-2241	8	27
β-strand	2245	1	30
α-helix	2249	1
β-strand	2250	1	29
α-helix	2251	1
β-strand	2252-2253	2	31
α-helix	2255-2258	4
β-strand	2267	1	32
β-strand	2278	1	32

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone-lysine N-methyltransferase ASH1L	A, B, C, D	protein	226	Homo sapiens	Q9NR48

Sequence of entity 1 (A, B, C, D), FASTA

>4YPA_1 Histone-lysine N-methyltransferase ASH1L (chains A, B, C, D)
GAMAGSYKKIRSNVYVDVKPLSGYEATTCNCKKPDDDTRKGCVDDCLNRMIFAECSPNTC
PCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNR
MIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSCDPNCEMQKWSVNGVYRIGLYAL
KDMPAGTELTYDYNFHSFNVEKAQLCKCGFEKCRGIIGGKSQRVNG

Ligands and cofactors

ID	Name	Formula	Copies
SAM	S-adenosylmethionine	C15 H22 N6 O5 S	4
ZN	Zinc ion	Zn	12

Primary citation

Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase. Rogawski, D.S., Ndoj, J., Cho, H.J. et al. Biochemistry (2015) 54:5401-5413. DOI 10.1021/acs.biochem.5b00697 · 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)
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)
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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