Research workbench
Crystal structure of porcine testicular carbonyl reductase/ 20BETA- hydroxysteroid dehydrogenase
Analyse Crystal structure of porcine testicular carbonyl reductase/ 20BETA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N5D
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonyl REDUCTASE/20BETA-hydroxysteroid dehydrogenase
- EC
- 1.1.1.53
- UniProt
- Q28960
- Ligands
- NDP, SO4
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonyl REDUCTASE/20BETA-hydroxysteroid dehydrogenase (EC 1.1.1.53) | protein | 288 | 47% helix, 15% strand | Q28960 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 551 | 0.71 | 0.80 | 62 | NDP |
| 2 | 57 | 0.30 | 0.76 | 15 | empty |
| 3 | 55 | 0.29 | 0.74 | 10 | empty |
Compared structures
- 1N5D · Crystal structure of porcine testicular carbonyl reductase/ 20BETA-hydroxysteroid… · the same entry in another collection · chain A against A, TM-score 1.00
- Q28960 · AlphaFold monomer V2.0 prediction for carbonyl reductase [NADPH] 1 (Q28960) · 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 Q28960
- Elsewhere: RCSB PDB 1N5D · PDBe 1N5D · UniProt Q28960
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