MolNFT v1 · #98646 · protein
Crystal structure of D-galactose-6-phosphate isomerase in a substrate- free form
4LFK · Galactose-6-phosphate isomerase subunit a: “Crystal structure of D-galactose-6-phosphate isomerase in a substrate- free form”. X-ray diffraction, 8 pockets (best druggability 0.72). MolNFT v1 #98646 on GenesisL1: 3D structure…
- PDB
- 4LFK
- Type
- protein
- Length
- 628 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galactose-6-phosphate isomerase subunit a; Galactose-6-phosphate isomerase subunit B
- EC
- 5.3.1.26
- UniProt
- C7TGZ6, C7TGZ5
- Pockets
- 8 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Galactose-6-phosphate isomerase subunit a (EC 5.3.1.26) | protein | 142 | 48% helix, 18% strand | C7TGZ6 |
| B, D | Galactose-6-phosphate isomerase subunit B (EC 5.3.1.26) | protein | 172 | 47% helix, 15% strand | C7TGZ5 |
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 | 52 | 0.72 | 0.99 | 15 | empty |
| 2 | 114 | 0.63 | 0.88 | 22 | empty |
| 3 | 105 | 0.59 | 0.86 | 22 | empty |
| 4 | 93 | 0.41 | 0.78 | 18 | empty |
| 5 | 126 | 0.38 | 0.74 | 23 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2052 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 2035 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 426 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 325 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 320 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4LFK · Crystal Structure of D-galactose-6-phosphate isomerase in a substrate-free 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 C7TGZ6
- Every structure of UniProt C7TGZ5
- Elsewhere: RCSB PDB 4LFK · PDBe 4LFK · UniProt C7TGZ6 · UniProt C7TGZ5
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