7BRE: MLL2

The crystal structure of MLL2 in complex with ASH2L and RBBP5. Determined by X-ray diffraction at 2.8 Å resolution. Released 22 Jul 2020.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 6
Atoms: 5,867
Mol. weight: 86.68 kDa
Ligands: SAH, ZN
Released: 22 Jul 2020

Explore 7BRE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7BRE contains 21 α-helices and 72 β-strands across 6 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: 2 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	446-451	6	2
β-strand	454-461	8	2
α-helix	463-465	3
β-strand	468	1	3
β-strand	469-475	7	1
β-strand	479-483	5	2
β-strand	498-499	2	2
α-helix	500-502	3

Chain B: 9 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2552-2554	3	4
α-helix	2559-2566	8
α-helix	2569-2576	8
β-strand	2577-2581	5	5
β-strand	2587-2591	5	5
β-strand	2595	1	6
β-strand	2600-2603	4	7
β-strand	2607-2610	4	8
α-helix	2611-2613	3
α-helix	2614-2624	11
β-strand	2630-2632	3	8
β-strand	2637-2640	4	8
β-strand	2644-2645	2	9
α-helix	2647-2650	4
α-helix	2651	1
β-strand	2652-2653	2	10
β-strand	2659-2666	8	7
β-strand	2669-2676	8	7
β-strand	2680	1	6
α-helix	2684	1
β-strand	2685	1	5
α-helix	2686	1
β-strand	2687-2688	2	10
α-helix	2692-2694	3
β-strand	2702	1	11
β-strand	2713	1	11

Chain C: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	337-338	2	9
β-strand	343-344	2	8

Chain D: 3 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	289-294	6	18
β-strand	299-300	2	19
β-strand	306-308	3	19
β-strand	314-318	5	18
β-strand	322	1	20
β-strand	325-335	11	19
β-strand	341-347	7	18
β-strand	363-367	5	18
β-strand	373-375	3	18
β-strand	378-380	3	18
β-strand	391-398	8	19
α-helix	399-401	3
β-strand	446-451	6	19
β-strand	454-461	8	19
α-helix	463-465	3
β-strand	468	1	20
β-strand	469-475	7	18
β-strand	479-482	4	19
β-strand	498-499	2	19
α-helix	500-502	3

Chain E: 7 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2552-2554	3	8
α-helix	2555-2557	3
α-helix	2559-2567	9
α-helix	2569-2576	8
β-strand	2577-2581	5	12
β-strand	2587-2591	5	12
β-strand	2595	1	13
β-strand	2600-2604	5	14
β-strand	2607-2610	4	4
α-helix	2613-2624	12
β-strand	2630-2632	3	4
β-strand	2637-2640	4	4
β-strand	2645	1	15
α-helix	2647-2650	4
α-helix	2651	1
β-strand	2652-2653	2	16
β-strand	2659-2665	7	14
β-strand	2670-2676	7	14
β-strand	2680	1	13
β-strand	2685	1	12
β-strand	2687-2688	2	16
α-helix	2692-2694	3
β-strand	2702	1	17
β-strand	2713	1	17

Chain F: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	338	1	15
β-strand	343-344	2	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Set1/Ash2 histone methyltransferase complex subunit ASH2	A, D	protein	184	Homo sapiens	Q9UBL3 (AlphaFold model)
Histone-lysine N-methyltransferase 2B	B, E	protein	165	Homo sapiens	Q9UMN6
Retinoblastoma-binding protein 5	C, F	protein	27	Homo sapiens	Q15291 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>7BRE_1 Set1/Ash2 histone methyltransferase complex subunit ASH2 (chains A, D)
SRVLLALHDRAPQLKISDDRLTVVGEKGYSMVRASHGVRKGAWYFEITVDEMPPDTAARL
GWSQPLGNLQAPLGYDKFSYSWRSKKGTKFHQSIGKHYSSGYGQGDVLGFYINLPEDTIS
GRGSSEIIFYKNGVNQGVAYKDIFEGVYFPAISLYKSCTVSINFGPCFKYPPKDLTYRPM
SDMG

Sequence of entity 2 (B, E), FASTA

>7BRE_2 Histone-lysine N-methyltransferase 2B (chains B, E)
STRRATSLELPMAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIR
SVLTDKREKFYDGKGIGCYMFRMDDFDVVDATMHGNAARFINHSCEPNCFSRVIHVEGQK
HIVIFALRRILRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN

Sequence of entity 3 (C, F), FASTA

>7BRE_3 Retinoblastoma-binding protein 5 (chains C, F)
SAFAPDFKELDENVEYEERESEFDIED

Ligands and cofactors

ID	Name	Formula	Copies
SAH	S-adenosyl-L-homocysteine	C14 H20 N6 O5 S	2
ZN	Zinc ion	Zn	2

Primary citation

Crystal Structure of MLL2 Complex Guides the Identification of a Methylation Site on P53 Catalyzed by KMT2 Family Methyltransferases. Li, Y., Zhao, L., Tian, X. et al. Structure (2020) 28:1141. DOI 10.1016/j.str.2020.07.002 · 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…
6E2H 2.24 Å, Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length…
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

Browse structure collections

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