3OPE: PDB entry 3OPE

Name: PDB 3OPE: Structural Basis of Auto-inhibitory mechanism of Histone methyltransferase
Published: 2011-01-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Structural Basis of Auto-inhibitory mechanism of Histone methyltransferase. Determined by X-ray diffraction at 2.9 Å resolution. Released 12 Jan 2011.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,391
Mol. weight: 52.56 kDa
Ligands: SAM, ZN
Released: 12 Jan 2011

Explore 3OPE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3OPE contains 16 α-helices and 38 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: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	2070-2071	2	1
β-strand	2076-2077	2	2
β-strand	2083	1	3
α-helix	2093-2095	3
α-helix	2111-2113	3
β-strand	2115	1	3
β-strand	2143-2146	4	4
β-strand	2152-2155	4	4
β-strand	2160	1	5
β-strand	2165-2168	4	3
β-strand	2172-2174	3	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	3
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	3
β-strand	2259	1	2
β-strand	2267	1	6
β-strand	2278	1	6

Chain B: 9 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2070-2071	2	7
β-strand	2076-2077	2	8
β-strand	2115	1	9
α-helix	2116-2118	3
α-helix	2125-2127	3
β-strand	2142-2146	5	10
β-strand	2152-2156	5	10
β-strand	2160	1	11
β-strand	2165-2168	4	9
β-strand	2172-2174	3	8
α-helix	2176-2182	7
α-helix	2183-2187	5
β-strand	2197	1	8
β-strand	2203-2205	3	8
β-strand	2209-2210	2	7
α-helix	2212-2215	4
α-helix	2216	1
β-strand	2217-2218	2	12
α-helix	2219	1
β-strand	2224-2231	8	9
β-strand	2234-2241	8	9
β-strand	2245	1	11
α-helix	2249	1
β-strand	2250-2251	2	10
β-strand	2252-2253	2	12
α-helix	2255-2258	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Probable histone-lysine N-methyltransferase ASH1L	A, B	protein	222	Homo sapiens	Q9NR48

Sequence of entity 1 (A, B), FASTA

>3OPE_1 Probable histone-lysine N-methyltransferase ASH1L (chains A, B)
GSYKKIRSNVYVDVKPLSGYEATTCNCKKPDDDTRKGCVDDCLNRMIFAECSPNTCPCGE
QCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQ
YHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSCDPNCEMQKWSVNGVYRIGLYALKDMP
AGTELTYDYNFHSFNVEKQQLCKCGFEKCRGIIGGKSQRVNG

Ligands and cofactors

ID	Name	Formula	Copies
SAM	S-adenosylmethionine	C15 H22 N6 O5 S	2
ZN	Zinc ion	Zn	6

Primary citation

Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism. An, S., Yeo, K.J., Jeon, Y.H. et al. J Biol Chem (2011) 286:8369-8374. DOI 10.1074/jbc.M110.203380 · 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)
6INE 2.6 Å, Crystal Structure of human ASH1L-MRG15 complex
4YNP 2.9 Å, ASH1L SET domain S2259M mutant in complex with S-adenosyl methionine (SAM)

Browse structure collections

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