Research workbench
The complex crystal structure of VREH2 mutant M263N with sno
Analyse The complex crystal structure of VREH2 mutant M263N with sno in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YB5
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epoxide hydrolase
- UniProt
- A0A0R5NGA4
- Ligands
- SNO
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Epoxide hydrolase | protein | 318 | 43% helix, 17% strand | A0A0R5NGA4 |
Ligands and binding sites
- SNO · (S)-para-nitrostyrene oxide · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.71 | 0.92 | 22 | empty |
| 2 | 256 | 0.66 | 0.83 | 29 | empty |
Compared structures
- 5YB5 · The complex crystal structure of VrEH2 mutant M263N with SNO · the same entry in another collection · chain B against B, 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 A0A0R5NGA4
- Elsewhere: RCSB PDB 5YB5 · PDBe 5YB5 · UniProt A0A0R5NGA4
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