MolNFT v2 · #160322 · protein
Structure of EBP and U18666A
6OHT · 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase: “Structure of EBP and U18666A”. X-ray diffraction at 3.2, 1 ligand (MKM), 10 pockets (best druggability 0.78). MolNFT v2 #160322 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6OHT
- Type
- protein
- Length
- 618 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.2
- Source
- Homo sapiens
- Molecule
- 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
- EC
- 5.3.3.5
- UniProt
- Q15125
- Ligands
- MKM
- Pockets
- 10 · best druggability 0.78
Structure
x-ray diffraction · resolution 3.2 · 1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase (EC 5.3.3.5) | protein | 206 | 70% helix, 0% strand | Q15125 |
Ligands and binding sites
- MKM · 3beta-(2-Diethylaminoethoxy)androst-5-en-17-one · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 448 | 0.78 | 0.86 | 39 | MKM |
| 2 | 423 | 0.76 | 0.84 | 38 | MKM |
| 3 | 440 | 0.76 | 0.84 | 40 | MKM |
| 4 | 128 | 0.44 | 0.75 | 17 | empty |
| 5 | 116 | 0.43 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1640 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
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 Q15125
- Elsewhere: RCSB PDB 6OHT · PDBe 6OHT · UniProt Q15125
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