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The crystal structure of 17-alpha hydroxysteroid dehydrogenase Y224D mutant.
Analyse The crystal structure of 17-alpha hydroxysteroid dehydrogenase Y224D mutant. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FJN
- Type
- protein
- Length
- 636 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldo-keto reductase family 1 member C21
- EC
- 1.1.1.209
- UniProt
- Q91WR5
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldo-keto reductase family 1 member C21 (EC 1.1.1.209) | protein | 315 | 39% helix, 17% strand | Q91WR5 |
| B | Aldo-keto reductase family 1 member C21 (EC 1.1.1.209) | protein | 321 | 39% helix, 15% strand | Q91WR5 |
Ligands and binding sites
- ACT · Acetate ion · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 811 | 0.78 | 0.81 | 81 | empty |
| 2 | 505 | 0.67 | 0.78 | 51 | ACT |
| 3 | 339 | 0.66 | 0.81 | 47 | empty |
| 4 | 250 | 0.64 | 0.82 | 35 | empty |
| 5 | 337 | 0.57 | 0.75 | 39 | ACT |
Interfaces
1 interface between chains.
- A–B · 912 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3FJN · The crystal structure of 17-alpha hydroxysteroid dehydrogenase Y224D mutant. · the same entry in another collection · chain A against A, TM-score 1.00
- Q91WR5 · AlphaFold monomer V2.0 prediction for aldo-keto reductase family 1 member C21 (Q91WR5) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q91WR5
- Elsewhere: RCSB PDB 3FJN · PDBe 3FJN · UniProt Q91WR5
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