Research workbench
Structure of a phosphoheptose isomerase from francisella tularensis
Analyse Structure of a phosphoheptose isomerase from francisella tularensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TRJ
- Type
- protein
- Length
- 743 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoheptose isomerase
- EC
- 5.-.-.-
- UniProt
- Q5NEF5
- Pockets
- 8 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 58% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Phosphoheptose isomerase (EC 5.-.-.-) | protein | 184 | 59% helix, 14% strand | Q5NEF5 |
| D | Phosphoheptose isomerase (EC 5.-.-.-) | protein | 191 | 57% helix, 13% strand | Q5NEF5 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.73 | 0.98 | 20 | empty |
| 2 | 70 | 0.73 | 0.98 | 25 | empty |
| 3 | 257 | 0.59 | 0.79 | 34 | empty |
| 4 | 157 | 0.50 | 0.78 | 21 | empty |
| 5 | 167 | 0.48 | 0.77 | 21 | empty |
Interfaces
6 interfaces between chains.
- A–D · 1721 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 1695 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 1055 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 974 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 657 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 17 modified (engineered).
Compared structures
- 3TRJ · Structure of a phosphoheptose isomerase from Francisella tularensis · 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 Q5NEF5
- Elsewhere: RCSB PDB 3TRJ · PDBe 3TRJ · UniProt Q5NEF5
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