Research workbench
Structure of the axin rgs-homologous domain in complex with a samp repeat from apc
Analyse Structure of the axin rgs-homologous domain in complex with a samp repeat from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EMU
- Type
- protein
- Length
- 148 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Axin; Adenomatous polyposis COLI protein
- UniProt
- O15169, P25054
Structure
x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Axin | protein | 132 | 73% helix, 0% strand | O15169 |
| B | Adenomatous polyposis COLI protein | protein | 16 | 63% helix, 0% strand | P25054 |
Ligands and binding sites
- GOL · Glycerol · additive · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 664 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1EMU · Structure of the axin rgs-homologous domain in complex with a samp repeat from apc · the same entry in another collection · chain A against A, TM-score 1.00
- O15169 · AlphaFold monomer V2.0 prediction for axin-1 (O15169) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O15169
- Every structure of UniProt P25054
- Elsewhere: RCSB PDB 1EMU · PDBe 1EMU · UniProt O15169 · UniProt P25054
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