Research workbench
Crystal structure of the erythromycin dehydratase
Analyse Crystal structure of the erythromycin dehydratase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EL6
- Type
- protein
- Length
- 271 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Erythromycin dehydratase
- EC
- 4.2.1.61
- UniProt
- Q03132
- Ligands
- SO4, CL
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythromycin dehydratase (EC 4.2.1.61) | protein | 271 | 18% helix, 41% strand | Q03132 |
Ligands and binding sites
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 | 215 | 0.67 | 0.84 | 37 | empty |
| 2 | 63 | 0.36 | 0.77 | 19 | empty |
Compared structures
- 3EL6 · Crystal Structure of the Erythromycin Dehydratase · 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 Q03132
- Elsewhere: RCSB PDB 3EL6 · PDBe 3EL6 · UniProt Q03132
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