Research workbench
Allosteric communication in the kix domain proceeds through dynamic re-packing of the hydrophobic core
Analyse Allosteric communication in the kix domain proceeds through dynamic re-packing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LXS
- Type
- protein
- Length
- 106 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Creb-binding protein; Histone-lysine N-methyltransferase mll
- EC
- 2.3.1.48, 2.1.1.43
- UniProt
- Q92793, Q03164
Structure
solution nmr · 2 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Creb-binding protein (EC 2.3.1.48) | protein | 87 | 74% helix, 0% strand | Q92793 |
| B | Histone-lysine N-methyltransferase mll (EC 2.1.1.43) | protein | 19 | 47% helix, 0% strand | Q03164 |
Interfaces
1 interface between chains.
- A–B · 850 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2LXS · Allosteric communication in the KIX domain proceeds through dynamic re-packing of the… · 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 A against A, TM-score 0.82
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 Q92793
- Every structure of UniProt Q03164
- Elsewhere: RCSB PDB 2LXS · PDBe 2LXS · UniProt Q92793 · UniProt Q03164
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