Research workbench
Crystal structure of TEAD4 in complex with a novel FAM181A peptide
Analyse Crystal structure of TEAD4 in complex with a novel FAM181A peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L9F
- Type
- protein
- Length
- 451 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional enhancer factor tef-3; Protein FAM181A
- UniProt
- Q62296, Q8N9Y4
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 4 distinct chains · 19% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional enhancer factor tef-3 | protein | 202 | 18% helix, 52% strand | Q62296 |
| C | Protein FAM181A | protein | 17 | 41% helix, 0% strand | Q8N9Y4 |
| B | Transcriptional enhancer factor tef-3 | protein | 216 | 17% helix, 50% strand | Q62296 |
| D | Protein FAM181A | protein | 16 | 25% helix, 0% strand | Q8N9Y4 |
Ligands and binding sites
- ACT · Acetate ion · additive · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 759 | 0.69 | 0.76 | 53 | ACT |
| 2 | 62 | 0.63 | 0.92 | 17 | empty |
| 3 | 75 | 0.62 | 0.90 | 21 | empty |
| 4 | 53 | 0.47 | 0.85 | 16 | empty |
| 5 | 59 | 0.25 | 0.72 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 848 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 739 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 735 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 6L9F · Crystal structure of TEAD4 in complex with a novel FAM181A peptide · the same entry in another collection · chain D against D, TM-score 1.00
- Q62296 · AlphaFold monomer V2.0 prediction for transcriptional enhancer factor tef-3 (Q62296) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q8N9Y4 · AlphaFold monomer V2.0 prediction for protein FAM181A (Q8N9Y4) · a predicted model of the same protein · chain C against A, TM-score 0.51
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 Q62296
- Every structure of UniProt Q8N9Y4
- Elsewhere: RCSB PDB 6L9F · PDBe 6L9F · UniProt Q62296 · UniProt Q8N9Y4
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