Research workbench
Crystal structure of phosphorylated ets-1 DNA binding and autoinhibitory domains (276-441)
Analyse Crystal structure of phosphorylated ets-1 DNA binding and autoinhibitory… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WU0
- Type
- protein
- Length
- 276 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein C-ets-1
- UniProt
- P14921
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein C-ets-1 | protein | 140 | 44% helix, 10% strand | P14921 |
| B | Protein C-ets-1 | protein | 136 | 48% helix, 9% strand | P14921 |
Interfaces
1 interface between chains.
- A–B · 725 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 3WU0 · Crystal structure of phosphorylated ETS-1 DNA binding and autoinhibitory domains (276-441) · the same entry in another collection · chain A against A, TM-score 1.00
- P14921 · AlphaFold monomer V2.0 prediction for protein C-ets-1 (P14921) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P14921
- Elsewhere: RCSB PDB 3WU0 · PDBe 3WU0 · UniProt P14921
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