Research workbench
Crystal structure of the DNA binding domain of human transcription factor FLI1
Analyse Crystal structure of the DNA binding domain of human transcription factor FLI1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5E8G
- Type
- protein
- Length
- 372 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Friend leukemia integration 1 transcription factor
- UniProt
- Q01543
- Ligands
- CO
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Friend leukemia integration 1 transcription factor | protein | 93 | 46% helix, 13% strand | Q01543 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 303 | 0.55 | 0.76 | 35 | empty |
Interfaces
3 interfaces between chains.
- B–D · 834 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 830 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 105 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5E8G · Crystal structure of the DNA binding domain of human transcription factor FLI1 · the same entry in another collection · chain D against D, TM-score 1.00
- Q01543 · AlphaFold monomer V2.0 prediction for friend leukemia integration 1 transcription factor… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q01543
- Elsewhere: RCSB PDB 5E8G · PDBe 5E8G · UniProt Q01543
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