Research workbench
AlphaFold monomer V2.0 prediction for cyclic AMP-responsive element- binding protein 1 (P15337)
Analyse AlphaFold monomer V2.0 prediction for cyclic AMP-responsive element- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P15337
- Type
- protein
- Length
- 327 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x70189663D9D82ce5dB28B4Fdc41ba0b8D3788BD3
- UniProt
- P15337
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 327 | — | P15337 |
Compared structures
- 1KDX · Kix domain of mouse cbp (creb binding protein) in complex with phosphorylated kinase… · an experimental structure of the same protein · chain A against B, TM-score 0.08
- 1KDX · Kix domain of mouse cbp (creb binding protein) in complex with phosphorylated kinase… · an experimental structure of the same protein · chain A against B, TM-score 0.08
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 P15337
- Elsewhere: UniProt P15337 · AlphaFold DB P15337
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