MolNFT v1 · #66295 · protein
Crystal structure of a chemotaxis protein chex (DDE_0281) from desulfovibrio desulfuricans subsp. at 1.30 a resolution
3HM4: “Crystal structure of a chemotaxis protein chex (DDE_0281) from desulfovibrio desulfuricans subsp. at 1.30 a…”. X-ray diffraction, 1 ligand (UNL), 1 pocket (best druggability 0.32). MolNFT v1 #66295 on GenesisL1: 3D structure…
- PDB
- 3HM4
- Type
- protein
- Length
- 303 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis protein chex
- UniProt
- Q316R4
- Ligands
- UNL
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemotaxis protein chex | protein | 153 | 37% helix, 33% strand | Q316R4 |
| B | Chemotaxis protein chex | protein | 150 | 37% helix, 35% strand | Q316R4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 50 | 0.32 | 0.77 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1328 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3HM4 · Crystal structure of a chemotaxis protein chex (DDE_0281) from desulfovibrio… · 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 Q316R4
- Elsewhere: RCSB PDB 3HM4 · PDBe 3HM4 · UniProt Q316R4
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