Research workbench
Crystal structure of CurK enoyl reductase
Analyse Crystal structure of CurK enoyl reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DP1
- Type
- protein
- Length
- 332 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.85
- Source
- Moorea producens 3L
- Molecule
- CurK
- UniProt
- F4Y425
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.82
Structure
x-ray diffraction · resolution 1.85 · 1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CurK | protein | 332 | 36% helix, 26% strand | F4Y425 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 374 | 0.82 | 0.91 | 46 | GOL |
| 2 | 109 | 0.65 | 0.88 | 17 | GOL |
| 3 | 121 | 0.44 | 0.77 | 25 | empty |
Compared structures
- 5DP1 · Crystal structure of curk enoyl reductase · 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 F4Y425
- Elsewhere: RCSB PDB 5DP1 · PDBe 5DP1 · UniProt F4Y425
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