Research workbench
Crystal structure of TFU_1878, a putative enoyl-CoA hydratase fromthermobifida fusca yx in complex with CoA
Analyse Crystal structure of TFU_1878, a putative enoyl-CoA hydratase fromthermobifida… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JVT
- Type
- protein
- Length
- 257 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
- Q47NQ8
- Ligands
- ACO
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-CoA hydratase (EC 4.2.1.17) | protein | 257 | 51% helix, 18% strand | Q47NQ8 |
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 | 156 | 0.55 | 0.80 | 23 | ACT |
| 2 | 202 | 0.48 | 0.75 | 32 | empty |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 4JVT · Crystal structure of Tfu_1878, a putative enoyl-CoA hydratase fromThermobifida fusca YX… · 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 Q47NQ8
- Elsewhere: RCSB PDB 4JVT · PDBe 4JVT · UniProt Q47NQ8
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