Research workbench
Domain-domain flexibility leads to allostery within the camp receptor protein (crp)
Analyse Domain-domain flexibility leads to allostery within the camp receptor protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RDI
- Type
- protein
- Length
- 400 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catabolite gene activator
- UniProt
- P0ACJ8
- Ligands
- CMP
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Catabolite gene activator | protein | 200 | 38% helix, 31% strand | P0ACJ8 |
Ligands and binding sites
- CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.77 | 0.96 | 23 | CMP |
| 2 | 109 | 0.76 | 0.96 | 24 | CMP |
| 3 | 215 | 0.69 | 0.85 | 24 | empty |
| 4 | 341 | 0.62 | 0.78 | 37 | empty |
| 5 | 175 | 0.49 | 0.77 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1587 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3RDI · Domain-domain flexibility leads to allostery within the camp receptor protein (CRP) · the same entry in another collection · chain A against A, TM-score 1.00
- P0ACJ8 · AlphaFold monomer V2.0 prediction for camp-activated global transcriptional regulator crp… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P0ACJ8
- Elsewhere: RCSB PDB 3RDI · PDBe 3RDI · UniProt P0ACJ8
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