MolNFT v1 · #96615 · protein
Crystal structure of enoyl-CoA hydrotase from deinococcus radiodurans R1
4JOT · Enoyl-CoA hydratase, putative: “Crystal structure of enoyl-CoA hydrotase from deinococcus radiodurans R1”. X-ray diffraction, 2 pockets (best druggability 0.53). MolNFT v1 #96615 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4JOT
- Type
- protein
- Length
- 255 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-CoA hydratase, putative
- UniProt
- Q9RY37
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-CoA hydratase, putative | protein | 255 | 51% helix, 19% strand | Q9RY37 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
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 | 126 | 0.53 | 0.81 | 24 | empty |
| 2 | 148 | 0.43 | 0.75 | 19 | empty |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 4JOT · Crystal structure of enoyl-CoA hydrotase from Deinococcus radiodurans R1 · 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 Q9RY37
- Elsewhere: RCSB PDB 4JOT · PDBe 4JOT · UniProt Q9RY37
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