Research workbench
Crystal structure of AKR4C16 bound with NADPH
Analyse Crystal structure of AKR4C16 bound with NADPH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7W1X
- Type
- protein
- Length
- 616 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AKR4-1
- UniProt
- A0A5J6VMF4
- Ligands
- NDP
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | AKR4-1 | protein | 308 | 41% helix, 17% strand | A0A5J6VMF4 |
| B | AKR4-1 | protein | 308 | 43% helix, 17% strand | A0A5J6VMF4 |
Ligands and binding sites
- NDP · Nadph dihydro-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
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 760 | 0.80 | 0.83 | 101 | NDP |
| 2 | 603 | 0.75 | 0.82 | 58 | empty |
Interfaces
1 interface between chains.
- A–B · 839 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7W1X · Crystal structure of AKR4C16 bound with NADPH · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A5J6VMF4
- Elsewhere: RCSB PDB 7W1X · PDBe 7W1X · UniProt A0A5J6VMF4
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