MolNFT v1 · #53837 · protein
Crystal structure of human TBX5 in the DNA-free form
2X6U · T-box transcription factor TBX5: “Crystal structure of human TBX5 in the DNA-free form”. X-ray diffraction, 1 ligand (MG), 1 pocket (best druggability 0.36). MolNFT v1 #53837 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2X6U
- Type
- protein
- Length
- 176 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-box transcription factor TBX5
- UniProt
- Q99593
- Ligands
- MG
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-box transcription factor TBX5 | protein | 176 | 16% helix, 40% strand | Q99593 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A
- PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 74 | 0.36 | 0.77 | 20 | empty |
Compared structures
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 Q99593
- Elsewhere: RCSB PDB 2X6U · PDBe 2X6U · UniProt Q99593
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