Research workbench
Crystal structure of the conserved hypothetical protein TTHA1091 from thermus thermophilus HB8
Analyse Crystal structure of the conserved hypothetical protein TTHA1091 from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VGG
- Type
- protein
- Length
- 966 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conserved hypothetical protein TT1634 (TTHA1091)
- UniProt
- Q5SJC3
- Pockets
- 8 · best druggability 0.89
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Conserved hypothetical protein TT1634 (TTHA1091) | protein | 161 | 31% helix, 34% strand | Q5SJC3 |
Pockets
8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 968 | 0.89 | 0.92 | 100 | empty |
| 2 | 323 | 0.81 | 0.92 | 38 | empty |
| 3 | 219 | 0.55 | 0.78 | 29 | empty |
| 4 | 204 | 0.54 | 0.78 | 21 | empty |
| 5 | 180 | 0.52 | 0.78 | 21 | empty |
Interfaces
15 interfaces between chains.
- E–F · 1917 Ų buried · 34 hydrogen bonds · protein-protein
- B–C · 1906 Ų buried · 31 hydrogen bonds · protein-protein
- D–E · 1900 Ų buried · 28 hydrogen bonds · protein-protein
- D–F · 1898 Ų buried · 30 hydrogen bonds · protein-protein
- A–C · 1891 Ų buried · 32 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 1VGG · Crystal Structure of the Conserved Hypothetical Protein TTHA1091 from Thermus… · 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 Q5SJC3
- Elsewhere: RCSB PDB 1VGG · PDBe 1VGG · UniProt Q5SJC3
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