Research workbench
Solution structure of the nuclear coactivator binding domain of cbp
Analyse Solution structure of the nuclear coactivator binding domain of cbp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KKJ
- Type
- protein
- Length
- 59 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Creb-binding protein
- EC
- 2.3.1.48
- UniProt
- P45481
Structure
solution nmr · 1 distinct chain · 58% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Creb-binding protein (EC 2.3.1.48) | protein | 59 | 58% helix, 0% strand | P45481 |
Compared structures
- 2KKJ · Solution structure of the Nuclear coactivator binding domain of CBP · the same entry in another collection · chain A against A, TM-score 1.00
- P45481 · AlphaFold monomer V2.0 prediction for histone lysine acetyltransferase crebbp (P45481) · a predicted model of the same protein · chain A against A, TM-score 0.45
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 P45481
- Elsewhere: RCSB PDB 2KKJ · PDBe 2KKJ · UniProt P45481
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