Research workbench
Structure of the phosphorylation motif of the oncogenic protein beta- catenin recognized by a selective monoclonal antibody
Analyse Structure of the phosphorylation motif of the oncogenic protein beta- catenin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G57
- Type
- protein
- Length
- 26 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-catenin
- UniProt
- P35222
- Ligands
- ACE, NH2
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-catenin | protein | 26 | 0% helix, 0% strand | P35222 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 modified, 1 covalent (phosphorylation, covalent ligand).
Compared structures
- 2G57 · Structure of the Phosphorylation Motif of the oncogenic Protein beta-Catenin Recognized… · the same entry in another collection · chain A against A, TM-score 1.00
- P35222 · AlphaFold monomer V2.0 prediction for catenin beta-1 (P35222) · a predicted model of the same protein · chain A against A, TM-score 0.35
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 P35222
- Elsewhere: RCSB PDB 2G57 · PDBe 2G57 · UniProt P35222
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