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Crystal structure of glucose-6-phosphate isomerase from elizabethkingia anophelis with bound glucose-6-phosphate
Analyse Crystal structure of glucose-6-phosphate isomerase from elizabethkingia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BZC
- Type
- protein
- Length
- 1,094 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
- A0A077EQ93
- Ligands
- G6P
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-6-phosphate isomerase (EC 5.3.1.9) | protein | 548 | 53% helix, 13% strand | A0A077EQ93 |
| B | Glucose-6-phosphate isomerase (EC 5.3.1.9) | protein | 546 | 54% helix, 12% strand | A0A077EQ93 |
Ligands and binding sites
- G6P · 6-O-phosphono-alpha-D-glucopyranose · sugar · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1074 | 0.79 | 0.80 | 75 | empty |
| 2 | 291 | 0.67 | 0.83 | 41 | G6P |
| 3 | 271 | 0.66 | 0.83 | 38 | G6P |
| 4 | 217 | 0.52 | 0.77 | 47 | EDO |
| 5 | 56 | 0.43 | 0.83 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 6371 Ų buried · 90 hydrogen bonds · protein-protein
Compared structures
- 6BZC · Crystal Structure of Glucose-6-phosphate Isomerase from Elizabethkingia anophelis with… · 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 A0A077EQ93
- Elsewhere: RCSB PDB 6BZC · PDBe 6BZC · UniProt A0A077EQ93
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