Research workbench
Crystal structure of FE(II) co-bound H-nox protein from C. subterraneus
Analyse Crystal structure of FE(II) co-bound H-nox protein from C. subterraneus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JRX
- Type
- protein
- Length
- 371 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-accepting chemotaxis protein
- UniProt
- Q8RBX6
- Ligands
- HEM, CMO
- Pockets
- 8 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyl-accepting chemotaxis protein | protein | 188 | 48% helix, 21% strand | Q8RBX6 |
| B | Methyl-accepting chemotaxis protein | protein | 183 | 52% helix, 20% strand | Q8RBX6 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- CMO · Carbon monoxide · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.85 | 0.94 | 37 | HEM, CMO |
| 2 | 256 | 0.83 | 0.94 | 35 | HEM, CMO |
| 3 | 129 | 0.43 | 0.76 | 25 | empty |
| 4 | 102 | 0.40 | 0.76 | 19 | empty |
| 5 | 75 | 0.38 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 731 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 cofactor (heme attachment).
Compared structures
- 5JRX · Crystal structure of Fe(II) CO-bound H-NOX protein from C. subterraneus · 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 Q8RBX6
- Elsewhere: RCSB PDB 5JRX · PDBe 5JRX · UniProt Q8RBX6
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