Research workbench
Crystal structure of pseudomonas aeruginosa phosphoheptose isomerase in complex with reaction product D-glycero-D-mannopyranose-7- phosphate
Analyse Crystal structure of pseudomonas aeruginosa phosphoheptose isomerase in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X92
- Type
- protein
- Length
- 391 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoheptose isomerase
- UniProt
- Q9HVZ0
- Ligands
- M7P
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoheptose isomerase | protein | 194 | 59% helix, 11% strand | Q9HVZ0 |
| B | Phosphoheptose isomerase | protein | 197 | 59% helix, 11% strand | Q9HVZ0 |
Ligands and binding sites
- M7P · 7-O-phosphono-D-glycero-alpha-D-manno-heptopyranose · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 360 | 0.54 | 0.74 | 58 | M7P |
| 2 | 107 | 0.42 | 0.78 | 21 | M7P |
Interfaces
1 interface between chains.
- A–B · 2020 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 1X92 · Crystal structure of pseudomonas aeruginosa phosphoheptose isomerase in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HVZ0 · AlphaFold monomer V2.0 prediction for phosphoheptose isomerase (Q9HVZ0) · a predicted model of the same protein · 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 Q9HVZ0
- Elsewhere: RCSB PDB 1X92 · PDBe 1X92 · UniProt Q9HVZ0
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