Research workbench
Structure of thermus thermophilus purs in the P21 form
Analyse Structure of thermus thermophilus purs in the P21 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DGB
- Type
- protein
- Length
- 332 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein purs
- UniProt
- Q72II0
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Hypothetical protein purs | protein | 83 | 33% helix, 41% strand | Q72II0 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1191 | 0.73 | 0.76 | 90 | empty |
Interfaces
4 interfaces between chains.
- B–C · 1344 Ų buried · 25 hydrogen bonds · protein-protein
- A–D · 1260 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 295 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 168 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2DGB · Structure of Thermus thermophilus PurS in the P21 Form · 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 Q72II0
- Elsewhere: RCSB PDB 2DGB · PDBe 2DGB · UniProt Q72II0
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