Research workbench
Crystal structure of MLLT1 (enl) yeats domain in complexed with piperazine-urea derivative 2
Analyse Crystal structure of MLLT1 (enl) yeats domain in complexed with piperazine-urea… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T1J
- Type
- protein
- Length
- 143 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein enl
- UniProt
- Q03111
- Ligands
- M7T
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein enl | protein | 143 | 8% helix, 50% strand | Q03111 |
Ligands and binding sites
- M7T · ~{N}-[[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-4-thiophen-2-ylcarbonyl-piperazine-1-carboxamide · ligand · chains A
- EDO · 1,2-ethanediol · additive · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6T1J · Crystal structure of MLLT1 (ENL) YEATS domain in complexed with piperazine-urea… · the same entry in another collection · chain A against A, TM-score 1.00
- Q03111 · AlphaFold monomer V2.0 prediction for protein enl (Q03111) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q03111
- Elsewhere: RCSB PDB 6T1J · PDBe 6T1J · UniProt Q03111
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