Research workbench
The mechanisms of hamp-mediated signaling in transmembrane receptors - the A291C mutant
Analyse The mechanisms of hamp-mediated signaling in transmembrane receptors - the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Y0Q
- Type
- protein
- Length
- 203 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- O28769
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 4 distinct chains · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 50 | 66% helix, 0% strand | O28769 |
| B | Uncharacterized protein | protein | 52 | 60% helix, 0% strand | O28769 |
| C | Uncharacterized protein | protein | 48 | 65% helix, 0% strand | O28769 |
| D | Uncharacterized protein | protein | 53 | 66% helix, 0% strand | O28769 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.30 | 0.74 | 13 | empty |
Interfaces
6 interfaces between chains.
- A–B · 967 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 837 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 372 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 339 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 120 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2Y0Q · The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291C mutant · the same entry in another collection · chain A against A, TM-score 1.00
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 O28769
- Elsewhere: RCSB PDB 2Y0Q · PDBe 2Y0Q · UniProt O28769
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