MolNFT v1 · #71157 · protein
Glucose-6-phosphate isomerase from francisella tularensis complexed with fructose-6-phosphate.
3M5P: “Glucose-6-phosphate isomerase from francisella tularensis complexed with fructose-6-phosphate.”. X-ray diffraction, 3 ligands (F6P, NA, PO4), 3 pockets (best druggability 0.63). MolNFT v1 #71157 on GenesisL1: 3D structure, binding…
- PDB
- 3M5P
- Type
- protein
- Length
- 542 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-6-phosphate isomerase
- EC
- 5.3.1.9
- UniProt
- Q5NFC4
- Ligands
- F6P, NA, PO4
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-6-phosphate isomerase (EC 5.3.1.9) | protein | 542 | 56% helix, 12% strand | Q5NFC4 |
Ligands and binding sites
- F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · chains A
- NA · Sodium ion · metal · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 344 | 0.63 | 0.79 | 42 | F6P |
| 2 | 56 | 0.48 | 0.85 | 16 | empty |
| 3 | 75 | 0.32 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 10 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 3M5P · Glucose-6-phosphate isomerase from Francisella tularensis complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5NFC4 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate isomerase (Q5NFC4) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q5NFC4
- Elsewhere: RCSB PDB 3M5P · PDBe 3M5P · UniProt Q5NFC4
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