Research workbench
Structural basis of p63a SAM domain mutants involved in AEC syndrome
Analyse Structural basis of p63a SAM domain mutants involved in AEC syndrome in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Y9U
- Type
- protein
- Length
- 67 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.6
- Source
- HOMO SAPIENS
- Molecule
- Tumor protein 63
- UniProt
- Q9H3D4
- Ligands
- SO4
Structure
x-ray diffraction · resolution 1.6 · 1 distinct chain · 64% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tumor protein 63 | protein | 67 | 64% helix, 3% strand | Q9H3D4 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q9H3D4
- Elsewhere: RCSB PDB 2Y9U · PDBe 2Y9U · UniProt Q9H3D4
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