Research workbench
The mechanisms of hamp-mediated signaling in transmembrane receptors - the A291I 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
- 2Y20
- Type
- protein
- Length
- 333 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- O28769
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 4 distinct chains · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 52 | 65% helix, 0% strand | O28769 |
| B | Uncharacterized protein | protein | 56 | 70% helix, 0% strand | O28769 |
| C, E, F | Uncharacterized protein | protein | 57 | 68% helix, 0% strand | O28769 |
| D | Uncharacterized protein | protein | 54 | 59% helix, 0% strand | O28769 |
Ligands and binding sites
- ZN · Zinc ion · metal · 9 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 257 | 0.58 | 0.79 | 36 | empty |
| 2 | 137 | 0.48 | 0.78 | 22 | empty |
| 3 | 144 | 0.43 | 0.75 | 24 | empty |
Interfaces
9 interfaces between chains.
- A–B · 859 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 857 Ų buried · 14 hydrogen bonds · protein-protein
- E–F · 850 Ų buried · 10 hydrogen bonds · protein-protein
- C–E · 369 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 201 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2Y20 · The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291I 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 2Y20 · PDBe 2Y20 · UniProt O28769
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