Research workbench
Crystal structure of conserved hypothetical protein, TTHA0132 from thermus thermophilus HB8
Analyse Crystal structure of conserved hypothetical protein, TTHA0132 from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DX6
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein TTHA0132
- UniProt
- Q5SM11
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hypothetical protein TTHA0132 | protein | 158 | 37% helix, 23% strand | Q5SM11 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 456 | 0.61 | 0.76 | 49 | empty |
| 2 | 91 | 0.53 | 0.84 | 25 | ACT, IPA |
| 3 | 80 | 0.50 | 0.83 | 25 | ACT |
Interfaces
1 interface between chains.
- A–B · 290 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 2DX6 · Crystal structure of conserved hypothetical protein, TTHA0132 from Thermus thermophilus… · 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 Q5SM11
- Elsewhere: RCSB PDB 2DX6 · PDBe 2DX6 · UniProt Q5SM11
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