Research workbench
The AER2 receptor from vibrio cholerae is a dual pas-heme oxygen sensor
Analyse The AER2 receptor from vibrio cholerae is a dual pas-heme oxygen sensor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CEQ
- Type
- protein
- Length
- 333 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-accepting chemotaxis protein
- UniProt
- A0A2D2BEZ7
- Ligands
- HEM
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Methyl-accepting chemotaxis protein | protein | 111 | 32% helix, 35% strand | A0A2D2BEZ7 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 3 copies · chains A, B, C
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 | 298 | 0.77 | 0.88 | 35 | HEM |
| 2 | 301 | 0.77 | 0.87 | 32 | HEM |
| 3 | 307 | 0.77 | 0.87 | 34 | HEM |
| 4 | 279 | 0.55 | 0.76 | 37 | empty |
| 5 | 83 | 0.36 | 0.76 | 20 | empty |
Interfaces
2 interfaces between chains.
- A–B · 817 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 451 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6CEQ · The Aer2 Receptor from Vibrio cholerae is a Dual PAS-Heme Oxygen Sensor · 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 A0A2D2BEZ7
- Elsewhere: RCSB PDB 6CEQ · PDBe 6CEQ · UniProt A0A2D2BEZ7
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