7W6A: MLL1 (N3861I/Q3867L/C3882SS)-RBBP5-ASH2L complex

Crystal structure of the MLL1 (N3861I/Q3867L/C3882SS)-RBBP5-ASH2L complex. Determined by X-ray diffraction at 2.21 Å resolution. Released 7 Sept 2022.

Method
X-ray diffraction
Resolution
2.21 Å
Organism
Homo sapiens
Chains
3
Atoms
2,988
Mol. weight
42.62 kDa
Ligands
ZN, SAH
Released
7 Sept 2022

Explore 7W6A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7W6A contains 12 α-helices and 35 β-strands across 3 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: 3 helices, 17 β-strands

ElementResiduesLengthSheet
β-strand289-29461
β-strand299-30022
β-strand306-30832
β-strand314-31851
β-strand32213
β-strand325-335112
β-strand341-34771
β-strand363-36751
β-strand373-37531
β-strand378-38031
β-strand391-39882
β-strand446-45162
β-strand454-46182
α-helix463-4653
β-strand46813
β-strand469-47571
β-strand479-48352
α-helix491-4922
β-strand498-49922
α-helix500-5034
Chain C: 9 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix3813-38153
α-helix3816-383015
β-strand3831-383554
β-strand3841-384554
β-strand384915
β-strand3854-385746
β-strand3861-386447
α-helix3867-387711
β-strand3885-388737
β-strand3892-389547
β-strand3899-390028
α-helix3902-39054
α-helix39061
β-strand3907-390829
β-strand3914-392186
β-strand3924-393186
β-strand393515
α-helix39391
β-strand3940-394124
β-strand3942-394329
α-helix3952-39543
α-helix39561
β-strand3957110
α-helix39581
β-strand3968110
Chain F: 0 helices, 2 β-strands
ElementResiduesLengthSheet
β-strand337-33828
β-strand343-34427

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Set1/Ash2 histone methyltransferase complex subunit ASH2Aprotein184Homo sapiensQ9UBL3 (AlphaFold model)
Histone-lysine N-methyltransferase 2ACprotein159Homo sapiensQ03164
Retinoblastoma-binding protein 5Fprotein27Homo sapiensQ15291 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>7W6A_1 Set1/Ash2 histone methyltransferase complex subunit ASH2 (chains A)
SRVLLALHDRAPQLKISDDRLTVVGEKGYSMVRASHGVRKGAWYFEITVDEMPPDTAARL
GWSQPLGNLQAPLGYDKFSYSWRSKKGTKFHQSIGKHYSSGYGQGDVLGFYINLPEDTIS
GRGSSEIIFYKNGVNQGVAYKDIFEGVYFPAISLYKSCTVSINFGPCFKYPPKDLTYRPM
SDMG
Sequence of entity 2 (C), FASTA
>7W6A_2 Histone-lysine N-methyltransferase 2A (chains C)
SDLPMPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGIVIRSILTDKR
EKYYDSKGIGSSYMFRIDDSEVVDATMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFA
MRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN
Sequence of entity 3 (F), FASTA
>7W6A_3 Retinoblastoma-binding protein 5 (chains F)
SAFAPDFKELDENVEYEERESEFDIED

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1
SAHS-adenosyl-L-homocysteineC14 H20 N6 O5 S1

Primary citation

Structural basis for product specificities of MLL family methyltransferases. Li, Y., Zhao, L., Zhang, Y. et al. Mol Cell (2022) 82:3810-3825.e8. DOI 10.1016/j.molcel.2022.08.022 · PubMed

Other PDB entries of the same protein (UniProt Q9UBL3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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