Research workbench
Crystal structure of enoyl-CoA HYDRATASE/ISOMERASE from cupriavidus metallidurans CH34
Analyse Crystal structure of enoyl-CoA HYDRATASE/ISOMERASE from cupriavidus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JCS
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-CoA HYDRATASE/ISOMERASE
- EC
- 4.2.1.17
- UniProt
- Q1LBW6
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-CoA HYDRATASE/ISOMERASE (EC 4.2.1.17) | protein | 265 | 51% helix, 15% strand | Q1LBW6 |
Pockets
2 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 | 0.66 | 0.80 | 32 | empty |
| 2 | 397 | 0.60 | 0.76 | 50 | empty |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 4JCS · Crystal structure of Enoyl-CoA hydratase/isomerase from Cupriavidus metallidurans CH34 · 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 Q1LBW6
- Elsewhere: RCSB PDB 4JCS · PDBe 4JCS · UniProt Q1LBW6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.