Research workbench
Crystal structure of aldo-keto reductase (AKR2E5) of the silkworm, bombyx mori
Analyse Crystal structure of aldo-keto reductase (AKR2E5) of the silkworm, bombyx mori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AZ0
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- H9JJU9
- Ligands
- CA
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 324 | 38% helix, 14% strand | H9JJU9 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- ACT · Acetate ion · additive · 8 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
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 | 480 | 0.70 | 0.80 | 44 | ACT |
| 2 | 71 | 0.35 | 0.77 | 18 | ACT |
Compared structures
- 5AZ0 · Crystal structure of aldo-keto reductase (AKR2E5) of the silkworm, Bombyx mori · 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 H9JJU9
- Elsewhere: RCSB PDB 5AZ0 · PDBe 5AZ0 · UniProt H9JJU9
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