MolNFT v1 · #15569 · protein
The crystal structure of phosphoglucose isomerase from rabbit muscle
1N8T · Glucose-6-phosphate isomerase: “The crystal structure of phosphoglucose isomerase from rabbit muscle”. X-ray diffraction, 10 pockets (best druggability 0.78). MolNFT v1 #15569 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1N8T
- Type
- protein
- Length
- 1,114 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-6-phosphate isomerase
- EC
- 5.3.1.9
- UniProt
- Q9N1E2
- Pockets
- 10 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glucose-6-phosphate isomerase (EC 5.3.1.9) | protein | 557 | 53% helix, 12% strand | Q9N1E2 |
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 967 | 0.78 | 0.80 | 65 | empty |
| 2 | 446 | 0.72 | 0.82 | 53 | empty |
| 3 | 521 | 0.72 | 0.81 | 53 | empty |
| 4 | 143 | 0.41 | 0.74 | 24 | empty |
| 5 | 51 | 0.40 | 0.82 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 6807 Ų buried · 91 hydrogen bonds · protein-protein
Compared structures
- 1N8T · The crystal structure of phosphoglucose isomerase from rabbit muscle · the same entry in another collection · chain A against A, TM-score 1.00
- Q9N1E2 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate isomerase (Q9N1E2) · a predicted model of the same protein · chain B 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 Q9N1E2
- Elsewhere: RCSB PDB 1N8T · PDBe 1N8T · UniProt Q9N1E2
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