Research workbench
Cryo-EM structure of human MLL1-ubncp complex (4.0 ångström)
Analyse Cryo-EM structure of human MLL1-ubncp complex (4.0 ångström) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KIV
- Type
- protein + DNA
- Length
- 2,154 residues
- Chains
- 15
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H3; Histone H4; Histone H2A; Histone H2B 1.1; DNA (145-mer); Histone-lysine…
- EC
- 2.1.1.43
- UniProt
- A0A310TTQ1, P62799, Q6AZJ8, P02281, Q03164, Q15291, P62979, Q9UBL3, P61964
- Ligands
- SAH, ZN
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 14 distinct chains · 26% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Histone H3 | protein | 97 | 63% helix, 3% strand | A0A310TTQ1 |
| B | Histone H4 | protein | 86 | 53% helix, 7% strand | P62799 |
| C | Histone H2A | protein | 112 | 48% helix, 3% strand | Q6AZJ8 |
| D | Histone H2B 1.1 | protein | 94 | 71% helix, 2% strand | P02281 |
| F | Histone H4 | protein | 81 | 64% helix, 4% strand | P62799 |
| G | Histone H2A | protein | 105 | 50% helix, 7% strand | Q6AZJ8 |
| H | Histone H2B 1.1 | protein | 95 | 74% helix, 4% strand | P02281 |
| I | DNA (145-mer) | dna | 145 | — | — |
| J | DNA (145-mer) | dna | 145 | — | — |
| K | Histone-lysine N-methyltransferase 2A (EC 2.1.1.43) | protein | 179 | 15% helix, 22% strand | Q03164 |
| N | Retinoblastoma-binding protein 5 | protein | 366 | 2% helix, 32% strand | Q15291 |
| O | Ubiquitin | protein | 76 | 22% helix, 26% strand | P62979 |
| T | SET1/ASH2 histone methyltransferase complex subunit ASH2 | protein | 176 | 2% helix, 26% strand | Q9UBL3 |
| R | Wd repeat-containing protein 5 | protein | 300 | 0% helix, 37% strand | P61964 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 935 | 0.80 | 0.82 | 58 | empty |
| 2 | 127 | 0.78 | 0.96 | 34 | empty |
| 3 | 663 | 0.78 | 0.83 | 77 | empty |
| 4 | 601 | 0.77 | 0.83 | 49 | empty |
| 5 | 662 | 0.77 | 0.82 | 70 | SAH |
Interfaces
51 interfaces between chains.
- I–J · 6607 Ų buried · 537 hydrogen bonds · nucleic-nucleic
- A–B · 2660 Ų buried · 17 hydrogen bonds · protein-protein
- E–F · 2612 Ų buried · 10 hydrogen bonds · protein-protein
- G–H · 2590 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 2584 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 6KIV · Cryo-EM structure of human MLL1-ubNCP complex (4.0 angstrom) · the same entry in another collection · chain R against R, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A310TTQ1
- Every structure of UniProt P62799
- Every structure of UniProt Q6AZJ8
- Every structure of UniProt P02281
- Every structure of UniProt Q03164
- Every structure of UniProt Q15291
- Every structure of UniProt P62979
- Every structure of UniProt Q9UBL3
- Every structure of UniProt P61964
- Elsewhere: RCSB PDB 6KIV · PDBe 6KIV · UniProt A0A310TTQ1 · UniProt P62799 · UniProt Q6AZJ8 · UniProt P02281 · UniProt Q03164 · UniProt Q15291 · UniProt P62979 · UniProt Q9UBL3 · UniProt P61964
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