Research workbench
Crystal structure of a probable enoyl-CoA hydratase from mycobacterium smegmatis
Analyse Crystal structure of a probable enoyl-CoA hydratase from mycobacterium smegmatis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OME
- Type
- protein
- Length
- 1,467 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-CoA hydratase
- EC
- 4.2.1.17
- UniProt
- A0R1R4
- Ligands
- ZN
- Pockets
- 12 · best druggability 0.86
Structure
x-ray diffraction · 5 distinct chains · 53% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-CoA hydratase (EC 4.2.1.17) | protein | 243 | 53% helix, 18% strand | A0R1R4 |
| B | Enoyl-CoA hydratase (EC 4.2.1.17) | protein | 242 | 53% helix, 17% strand | A0R1R4 |
| C | Enoyl-CoA hydratase (EC 4.2.1.17) | protein | 247 | 52% helix, 17% strand | A0R1R4 |
| D, E | Enoyl-CoA hydratase (EC 4.2.1.17) | protein | 244 | 53% helix, 17% strand | A0R1R4 |
| F | Enoyl-CoA hydratase (EC 4.2.1.17) | protein | 247 | 52% helix, 17% strand | A0R1R4 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 883 | 0.86 | 0.88 | 96 | empty |
| 2 | 916 | 0.86 | 0.88 | 87 | empty |
| 3 | 1116 | 0.79 | 0.81 | 84 | empty |
| 4 | 1113 | 0.79 | 0.81 | 82 | empty |
| 5 | 1151 | 0.79 | 0.81 | 84 | empty |
Interfaces
15 interfaces between chains.
- D–F · 1328 Ų buried · 15 hydrogen bonds · protein-protein
- D–E · 1327 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1313 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 1305 Ų buried · 14 hydrogen bonds · protein-protein
- E–F · 1305 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 3OME · Crystal structure of a probable ENOYL-COA Hydratase from Mycobacterium Smegmatis · 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 A0R1R4
- Elsewhere: RCSB PDB 3OME · PDBe 3OME · UniProt A0R1R4
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