Research workbench
17BETA-hydroxysteroid dehydrogenase 14 variant T205 in complex with a non-steroidal inhibitor.
Analyse 17BETA-hydroxysteroid dehydrogenase 14 variant T205 in complex with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5L7Y
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 17-beta-hydroxysteroid dehydrogenase 14
- EC
- 1.1.1.-
- UniProt
- Q9BPX1
- Ligands
- 6QO, NAD, NA
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 17-beta-hydroxysteroid dehydrogenase 14 (EC 1.1.1.-) | protein | 256 | 51% helix, 15% strand | Q9BPX1 |
Ligands and binding sites
- 6QO · (4-fluoranyl-3-oxidanyl-phenyl)-[6-(2-fluoranyl-3-oxidanyl-phenyl)pyridin-2-yl]methanone · ligand · 2 copies · chains A
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 645 | 0.77 | 0.82 | 62 | NAD, 6QO |
Compared structures
- 5L7Y · 17beta-hydroxysteroid dehydrogenase 14 variant T205 in complex with a non-steroidal… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BPX1 · AlphaFold monomer V2.0 prediction for 17-beta-hydroxysteroid dehydrogenase 14 (Q9BPX1) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9BPX1
- Elsewhere: RCSB PDB 5L7Y · PDBe 5L7Y · UniProt Q9BPX1
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