Research workbench
Solution structure of MLL1 PHD3-CYP33 rrm chimeric protein
Analyse Solution structure of MLL1 PHD3-CYP33 rrm chimeric protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KU7
- Type
- protein
- Length
- 140 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MLL1 PHD3-CYP33 rrm chimeric protein
- UniProt
- Q03164, Q9UNP9
- Pockets
- 1 · best druggability 0.37
Structure
solution nmr · 1 distinct chain · 24% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MLL1 PHD3-CYP33 rrm chimeric protein | protein | 140 | 24% helix, 19% strand | Q03164, Q9UNP9 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.37 | 0.74 | 24 | empty |
Compared structures
- 2KU7 · Solution structure of MLL1 PHD3-Cyp33 RRM chimeric protein · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UNP9 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase E (Q9UNP9) · a predicted model of the same protein · chain A against A, TM-score 0.53
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 Q03164
- Every structure of UniProt Q9UNP9
- Elsewhere: RCSB PDB 2KU7 · PDBe 2KU7 · UniProt Q03164 · UniProt Q9UNP9
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