Research workbench
Structural diversity in cbp P160 complexes
Analyse Structural diversity in cbp P160 complexes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C52
- Type
- protein
- Length
- 117 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Creb-binding protein; Nuclear receptor coactivator 1
- EC
- 2.3.1.48
- UniProt
- P45481, Q15788
Structure
solution nmr · 2 distinct chains · 44% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Creb-binding protein (EC 2.3.1.48) | protein | 58 | 57% helix, 0% strand | P45481 |
| B | Nuclear receptor coactivator 1 (EC 2.3.1.48) | protein | 59 | 32% helix, 0% strand | Q15788 |
Interfaces
1 interface between chains.
- A–B · 996 Ų buried · 10 hydrogen bonds · protein-protein
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 P45481
- Every structure of UniProt Q15788
- Elsewhere: RCSB PDB 2C52 · PDBe 2C52 · UniProt P45481 · UniProt Q15788
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