Research workbench
Crystal structure of diels-alderase CE11
Analyse Crystal structure of diels-alderase CE11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O5S
- Type
- protein
- Length
- 635 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diisopropyl-fluorophosphatase
- EC
- 3.1.8.2
- UniProt
- Q7SIG4
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diisopropyl-fluorophosphatase (EC 3.1.8.2) | protein | 323 | 6% helix, 49% strand | Q7SIG4 |
| B | Diisopropyl-fluorophosphatase (EC 3.1.8.2) | protein | 312 | 3% helix, 50% strand | Q7SIG4 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.78 | 0.98 | 33 | empty |
| 2 | 93 | 0.76 | 0.97 | 26 | empty |
| 3 | 201 | 0.71 | 0.87 | 22 | empty |
| 4 | 173 | 0.70 | 0.88 | 27 | empty |
Compared structures
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 Q7SIG4
- Elsewhere: RCSB PDB 4O5S · PDBe 4O5S · UniProt Q7SIG4
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