Research workbench
Crystal structure of helicobacter pylori tlpa chemoreceptor ligand binding domain
Analyse Crystal structure of helicobacter pylori tlpa chemoreceptor ligand binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E09
- Type
- protein
- Length
- 1,012 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-accepting chemotaxis protein tlpa
- UniProt
- A0A1U9IS38
- Pockets
- 12 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyl-accepting chemotaxis protein tlpa | protein | 256 | 38% helix, 34% strand | A0A1U9IS38 |
| B | Methyl-accepting chemotaxis protein tlpa | protein | 241 | 37% helix, 31% strand | A0A1U9IS38 |
| C | Methyl-accepting chemotaxis protein tlpa | protein | 255 | 39% helix, 31% strand | A0A1U9IS38 |
| D | Methyl-accepting chemotaxis protein tlpa | protein | 260 | 38% helix, 32% strand | A0A1U9IS38 |
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.74 | 0.98 | 15 | empty |
| 2 | 56 | 0.73 | 0.98 | 15 | empty |
| 3 | 59 | 0.73 | 0.97 | 15 | empty |
| 4 | 56 | 0.72 | 0.97 | 15 | empty |
| 5 | 766 | 0.72 | 0.78 | 55 | empty |
Interfaces
4 interfaces between chains.
- A–D · 1035 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 1032 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 254 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 42 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 39 modified (engineered).
Compared structures
- 6E09 · Crystal Structure of Helicobacter pylori TlpA Chemoreceptor Ligand Binding Domain · 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 A0A1U9IS38
- Elsewhere: RCSB PDB 6E09 · PDBe 6E09 · UniProt A0A1U9IS38
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