MolNFT v1 · #110110 · protein
Crystal structure of the sensory domain of the campylobacter jejuni chemoreceptor TLP3 (ccml) with isoleucine bound.
4XMR · Putative methyl-accepting chemotaxis signal transduction…: “Crystal structure of the sensory domain of the campylobacter jejuni chemoreceptor TLP3 (ccml) with isoleucine…”. X-ray diffraction, 2 ligands (ILE, SO4), 7 pockets (best…
- PDB
- 4XMR
- Type
- protein
- Length
- 497 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative methyl-accepting chemotaxis signal transduction protein
- UniProt
- Q0P864
- Ligands
- ILE, SO4
- Pockets
- 7 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative methyl-accepting chemotaxis signal transduction protein | protein | 245 | 42% helix, 29% strand | Q0P864 |
| B | Putative methyl-accepting chemotaxis signal transduction protein | protein | 252 | 42% helix, 28% strand | Q0P864 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 791 | 0.74 | 0.79 | 56 | empty |
| 2 | 51 | 0.62 | 0.93 | 14 | ILE |
| 3 | 208 | 0.55 | 0.78 | 26 | empty |
| 4 | 64 | 0.54 | 0.87 | 17 | empty |
| 5 | 117 | 0.50 | 0.80 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 949 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4XMR · Crystal structure of the sensory domain of the Campylobacter jejuni chemoreceptor Tlp3… · 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 Q0P864
- Elsewhere: RCSB PDB 4XMR · PDBe 4XMR · UniProt Q0P864
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