MolNFT v1 · #117445 · protein
Crystal structure of the DNA binding domain of human transcription factor FLI1
5E8G · Friend leukemia integration 1 transcription factor: “Crystal structure of the DNA binding domain of human transcription factor FLI1”. X-ray diffraction, 1 ligand (CO), 1 pocket (best druggability 0.55). MolNFT v1 #117445 on…
- 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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