Research workbench
Crystal structure of carnitinyl-CoA hydratase from mycobacterium avium
Analyse Crystal structure of carnitinyl-CoA hydratase from mycobacterium avium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3R0O
- Type
- protein
- Length
- 785 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carnitinyl-CoA dehydratase
- EC
- 4.2.1.-
- UniProt
- A0QFV0
- Ligands
- K
- Pockets
- 8 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Carnitinyl-CoA dehydratase (EC 4.2.1.-) | protein | 262 | 46% helix, 18% strand | A0QFV0 |
| B | Carnitinyl-CoA dehydratase (EC 4.2.1.-) | protein | 261 | 46% helix, 18% strand | A0QFV0 |
Ligands and binding sites
- K · Potassium ion · metal · chains C
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B, C
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1188 | 0.82 | 0.83 | 131 | EDO |
| 2 | 426 | 0.65 | 0.78 | 44 | GOL |
| 3 | 385 | 0.63 | 0.77 | 43 | K |
| 4 | 394 | 0.60 | 0.76 | 41 | empty |
| 5 | 102 | 0.40 | 0.76 | 19 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1465 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 1451 Ų buried · 24 hydrogen bonds · protein-protein
- A–C · 1444 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 3R0O · Crystal structure of carnitinyl-CoA hydratase from Mycobacterium avium · 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 A0QFV0
- Elsewhere: RCSB PDB 3R0O · PDBe 3R0O · UniProt A0QFV0
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