Research workbench
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins
Analyse Structure and dynamics conspire in the evolution of affinity between… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ES7
- Type
- protein
- Length
- 94 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nuclear receptor coactivator 3; Creb-binding protein
- EC
- 2.3.1.48
- UniProt
- Q9Y6Q9, Q92793
- Pockets
- 1 · best druggability 0.77
Structure
solution nmr · 2 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear receptor coactivator 3 (EC 2.3.1.48) | protein | 44 | 64% helix, 0% strand | Q9Y6Q9 |
| B | Creb-binding protein (EC 2.3.1.48) | protein | 50 | 74% helix, 0% strand | Q92793 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.77 | 0.95 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1557 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6ES7 · Structure and dynamics conspire in the evolution of affinity between intrinsically… · the same entry in another collection · chain A against A, TM-score 1.00
- Q92793 · AlphaFold monomer V2.0 prediction for creb-binding protein (Q92793) · a predicted model of the same protein · chain B against A, TM-score 0.55
- Q9Y6Q9 · AlphaFold monomer V2.0 prediction for nuclear receptor coactivator 3 (Q9Y6Q9) · a predicted model of the same protein · chain A against A, TM-score 0.34
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 Q9Y6Q9
- Every structure of UniProt Q92793
- Elsewhere: RCSB PDB 6ES7 · PDBe 6ES7 · UniProt Q9Y6Q9 · UniProt Q92793
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