Research workbench
3-alpha-HYDROXYSTEROID/DIHYDRODIOL dehydrogenase from rattus norvegicus
Analyse 3-alpha-HYDROXYSTEROID/DIHYDRODIOL dehydrogenase from rattus norvegicus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LWI
- Type
- protein
- Length
- 610 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-alpha-HYDROXYSTEROID/DIHYDRODIOL dehydrogenase
- EC
- 1.1.1.213
- UniProt
- P23457
- Ligands
- NAP
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 3-alpha-HYDROXYSTEROID/DIHYDRODIOL dehydrogenase (EC 1.1.1.213) | protein | 305 | 40% helix, 17% strand | P23457 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 768 | 0.72 | 0.77 | 76 | NAP |
| 2 | 462 | 0.70 | 0.80 | 45 | NAP |
| 3 | 136 | 0.38 | 0.73 | 31 | empty |
| 4 | 63 | 0.32 | 0.76 | 18 | empty |
| 5 | 50 | 0.28 | 0.75 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1204 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1LWI · 3-alpha-HYDROXYSTEROID/DIHYDRODIOL dehydrogenase from rattus norvegicus · the same entry in another collection · chain A against A, TM-score 1.00
- P23457 · AlphaFold monomer V2.0 prediction for 3-alpha-hydroxysteroid dehydrogenase (P23457) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P23457
- Elsewhere: RCSB PDB 1LWI · PDBe 1LWI · UniProt P23457
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