Research workbench
X-ray structure of human soluble epoxide hydrolase C-terminal domain (hseh CTD)IN complex with 15D-PGJ2
Analyse X-ray structure of human soluble epoxide hydrolase C-terminal domain (hseh… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6I5G
- Type
- protein
- Length
- 632 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
- PTG
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bifunctional epoxide hydrolase 2 (EC 3.3.2.10, 3.1.3.76) | protein | 316 | 44% helix, 16% strand | P34913 |
Ligands and binding sites
- PTG · (5E,14E)-11-oxoprosta-5,9,12,14-tetraen-1-oic acid · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 12 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 431 | 0.79 | 0.87 | 35 | empty |
| 2 | 453 | 0.77 | 0.85 | 39 | empty |
| 3 | 165 | 0.74 | 0.91 | 25 | PTG |
| 4 | 176 | 0.72 | 0.89 | 25 | PTG |
| 5 | 478 | 0.63 | 0.76 | 43 | EDO |
Interfaces
1 interface between chains.
- A–B · 342 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6I5G · X-ray structure of human soluble Epoxide Hydrolase C-terminal Domain (hsEH CTD)in complex… · 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 6I5G · PDBe 6I5G · UniProt P34913
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