Research workbench
Crystal structure of perakine reductase, founder member of a novel akr subfamily with unique conformational changes during NADPH binding
Analyse Crystal structure of perakine reductase, founder member of a novel akr… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V0U
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Perakine reductase
- UniProt
- Q3L181
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Perakine reductase | protein | 282 | 43% helix, 18% strand | Q3L181 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.49 | 0.78 | 22 | empty |
Compared structures
- 3V0U · Crystal Structure of Perakine Reductase, Founder Member of a Novel AKR Subfamily with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q3L181 · AlphaFold monomer V2.0 prediction for perakine reductase (Q3L181) · 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 Q3L181
- Elsewhere: RCSB PDB 3V0U · PDBe 3V0U · UniProt Q3L181
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