Research workbench
Crystal structure of putative enoyl-CoA HYDRATASE/ISOMERASE from novosphingobium aromaticivorans dsm 12444
Analyse Crystal structure of putative enoyl-CoA HYDRATASE/ISOMERASE from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JYJ
- Type
- protein
- Length
- 538 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-CoA HYDRATASE/ISOMERASE
- UniProt
- Q2GB08
- Ligands
- UNL
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-CoA HYDRATASE/ISOMERASE | protein | 270 | 52% helix, 15% strand | Q2GB08 |
| B | Enoyl-CoA HYDRATASE/ISOMERASE | protein | 268 | 53% helix, 15% strand | Q2GB08 |
Ligands and binding sites
- UNL · Unknown ligand · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 916 | 0.79 | 0.81 | 73 | empty |
| 2 | 314 | 0.72 | 0.84 | 42 | UNL |
| 3 | 380 | 0.71 | 0.82 | 40 | UNL |
| 4 | 130 | 0.46 | 0.77 | 24 | empty |
| 5 | 139 | 0.44 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 856 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 4JYJ · Crystal Structure of putative enoyl-CoA hydratase/isomerase from Novosphingobium… · 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 Q2GB08
- Elsewhere: RCSB PDB 4JYJ · PDBe 4JYJ · UniProt Q2GB08
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