Research workbench
Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with C9
Analyse Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with C9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C4X
- Type
- protein
- Length
- 627 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional epoxide hydrolase 2
- EC
- 3.3.2.10, 3.1.3.76
- UniProt
- P34913
- Ligands
- W9M
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional epoxide hydrolase 2 (EC 3.3.2.10, 3.1.3.76) | protein | 313 | 40% helix, 17% strand | P34913 |
| B | Bifunctional epoxide hydrolase 2 (EC 3.3.2.10, 3.1.3.76) | protein | 314 | 39% helix, 16% strand | P34913 |
Ligands and binding sites
- W9M · 3-(3,4-dichlorophenyl)-1,1-dimethyl-urea · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 592 | 0.82 | 0.87 | 56 | W9M |
| 2 | 554 | 0.82 | 0.87 | 50 | W9M |
| 3 | 52 | 0.56 | 0.90 | 15 | empty |
| 4 | 92 | 0.36 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 792 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4C4X · Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with C9 · 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 P34913
- Elsewhere: RCSB PDB 4C4X · PDBe 4C4X · UniProt P34913
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