Research workbench
Crystal structure of TT0030 from thermus thermophilus
Analyse Crystal structure of TT0030 from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IEL
- Type
- protein
- Length
- 259 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein TT0030
- UniProt
- Q72LM7
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein TT0030 | protein | 132 | 41% helix, 23% strand | Q72LM7 |
| B | Hypothetical protein TT0030 | protein | 127 | 43% helix, 23% strand | Q72LM7 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.78 | 0.94 | 26 | empty |
| 2 | 105 | 0.58 | 0.86 | 23 | empty |
| 3 | 68 | 0.30 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1446 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 2IEL · CRYSTAL STRUCTURE OF TT0030 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 Q72LM7
- Elsewhere: RCSB PDB 2IEL · PDBe 2IEL · UniProt Q72LM7
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