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The structure of wild-type human HADH2 (17BETA-hydroxysteroid dehydrogenase type 10) bound to NAD+ at 1.2 a
Analyse The structure of wild-type human HADH2 (17BETA-hydroxysteroid dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O23
- Type
- protein
- Length
- 503 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HADH2 protein
- EC
- 1.1.1.178
- UniProt
- Q6IBS9
- Ligands
- NAD
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HADH2 protein (EC 1.1.1.178) | protein | 248 | 43% helix, 18% strand | Q6IBS9 |
| B | HADH2 protein (EC 1.1.1.178) | protein | 255 | 42% helix, 17% strand | Q6IBS9 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 392 | 0.70 | 0.82 | 50 | NAD |
| 2 | 352 | 0.62 | 0.78 | 39 | NAD |
| 3 | 78 | 0.39 | 0.78 | 25 | empty |
| 4 | 115 | 0.37 | 0.74 | 19 | GOL |
Interfaces
1 interface between chains.
- A–B · 1686 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 2O23 · The structure of wild-type human HADH2 (17beta-hydroxysteroid dehydrogenase type 10)… · 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 Q6IBS9
- Elsewhere: RCSB PDB 2O23 · PDBe 2O23 · UniProt Q6IBS9
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