MolNFT v1 · #24054 · protein
Crystal structure of enoyl-CoA hydratase from thermus thermophilus HB8
1UIY: “Crystal structure of enoyl-CoA hydratase from thermus thermophilus HB8”. X-ray diffraction, 3 pockets (best druggability 0.70). MolNFT v1 #24054 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1UIY
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-CoA hydratase
- EC
- 4.2.1.17
- UniProt
- P83702
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-CoA hydratase (EC 4.2.1.17) | protein | 253 | 56% helix, 15% strand | P83702 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 466 | 0.70 | 0.80 | 44 | GOL |
| 2 | 167 | 0.49 | 0.77 | 27 | empty |
| 3 | 52 | 0.37 | 0.80 | 14 | empty |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 1UIY · Crystal Structure of Enoyl-CoA Hydratase from Thermus Thermophilus HB8 · 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 P83702
- Elsewhere: RCSB PDB 1UIY · PDBe 1UIY · UniProt P83702
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