Research workbench
Crystal structure of the mtb enoyl CoA isomerase in complex with hydroxyhexanoyl CoA
Analyse Crystal structure of the mtb enoyl CoA isomerase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FND
- Type
- protein
- Length
- 232 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-CoA HYDRATASE/ISOMERASE family protein
- EC
- 4.2.1.17
- UniProt
- P96907
- Ligands
- 3H9, SO4
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-CoA HYDRATASE/ISOMERASE family protein (EC 4.2.1.17) | protein | 232 | 50% helix, 16% strand | P96907 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 144 | 0.60 | 0.83 | 25 | empty |
Compared structures
- 4FND · Crystal structure of the Mtb enoyl CoA isomerase in complex with hydroxyhexanoyl CoA · 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 P96907
- Elsewhere: RCSB PDB 4FND · PDBe 4FND · UniProt P96907
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