Research workbench
Crystal structure of the holo form of AKR4C7 from maize
Analyse Crystal structure of the holo form of AKR4C7 from maize in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JH2
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldose reductase, AKR4C7
- UniProt
- A2T1W7
- Ligands
- A2P, CL
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldose reductase, AKR4C7 | protein | 257 | 45% helix, 17% strand | A2T1W7 |
Ligands and binding sites
- A2P · Adenosine-2'-5'-diphosphate · ligand · chains A
- CL · Chloride ion · ion · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.40 | 0.78 | 18 | empty |
| 2 | 67 | 0.30 | 0.74 | 21 | empty |
Compared structures
- 5JH2 · Crystal structure of the holo form of AKR4C7 from maize · 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 A2T1W7
- Elsewhere: RCSB PDB 5JH2 · PDBe 5JH2 · UniProt A2T1W7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.