Research workbench
Structural and biochemical insights into MLL1 core complex assembly and regulation.
Analyse Structural and biochemical insights into MLL1 core complex assembly and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P4F
- Type
- protein
- Length
- 322 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wd repeat-containing protein 5; Retinoblastoma-binding protein 5; Histone-lysine…
- EC
- 2.1.1.43
- UniProt
- P61964, Q15291, Q03164
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 1% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wd repeat-containing protein 5 | protein | 304 | 0% helix, 51% strand | P61964 |
| B | Retinoblastoma-binding protein 5 | protein | 9 | 0% helix, 0% strand | Q15291 |
| C | Histone-lysine N-methyltransferase mll (EC 2.1.1.43) | protein | 9 | 33% helix, 0% strand | Q03164 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 519 | 0.74 | 0.82 | 45 | empty |
Interfaces
2 interfaces between chains.
- A–C · 543 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 508 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3P4F · Structural and biochemical insights into MLL1 core complex assembly and regulation. · the same entry in another collection · chain A against A, TM-score 1.00
- Q15291 · AlphaFold monomer V2.0 prediction for retinoblastoma-binding protein 5 (Q15291) · a predicted model of the same protein · chain B against A, TM-score 0.62
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 P61964
- Every structure of UniProt Q15291
- Every structure of UniProt Q03164
- Elsewhere: RCSB PDB 3P4F · PDBe 3P4F · UniProt P61964 · UniProt Q15291 · UniProt Q03164
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