MolNFT v1 · #117929 · protein
Crystal structure of the palmitoylated human TEAD3 transcription factor
5EMW · Transcriptional enhancer factor tef-5: “Crystal structure of the palmitoylated human TEAD3 transcription factor”. X-ray diffraction, 1 ligand (CA), 8 pockets (best druggability 0.76). MolNFT v1 #117929 on GenesisL1: 3D structure…
- PDB
- 5EMW
- Type
- protein
- Length
- 830 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional enhancer factor tef-5
- UniProt
- Q99594
- Ligands
- CA
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 3 distinct chains · 17% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional enhancer factor tef-5 | protein | 208 | 17% helix, 52% strand | Q99594 |
| B, D | Transcriptional enhancer factor tef-5 | protein | 207 | 17% helix, 52% strand | Q99594 |
| C | Transcriptional enhancer factor tef-5 | protein | 208 | 16% helix, 52% strand | Q99594 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1199 | 0.76 | 0.78 | 93 | empty |
| 2 | 696 | 0.69 | 0.77 | 69 | CA |
| 3 | 672 | 0.68 | 0.76 | 57 | CA |
| 4 | 314 | 0.66 | 0.82 | 34 | empty |
| 5 | 324 | 0.62 | 0.79 | 37 | empty |
Interfaces
5 interfaces between chains.
- A–C · 804 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 730 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 661 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 251 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 249 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard).
Compared structures
- 5EMW · Crystal structure of the palmitoylated human TEAD3 transcription factor · the same entry in another collection · chain A against A, TM-score 1.00
- Q99594 · AlphaFold monomer V2.0 prediction for transcriptional enhancer factor tef-5 (Q99594) · a predicted model of the same protein · chain B 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 Q99594
- Elsewhere: RCSB PDB 5EMW · PDBe 5EMW · UniProt Q99594
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