MolNFT v1 · #86034 · protein
The complex structure of the bacterial aldo-keto reductase AKR14A1 with NADP and citrate
4AUB: “The complex structure of the bacterial aldo-keto reductase AKR14A1 with NADP and citrate”. X-ray diffraction, 1 ligand (NAP), 20 pockets (best druggability 0.84). MolNFT v1 #86034 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4AUB
- Type
- protein
- Length
- 2,512 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldo-keto reductase AKR14A1
- UniProt
- Q46851
- Ligands
- NAP
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 8 distinct chains · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldo-keto reductase AKR14A1 | protein | 312 | 43% helix, 15% strand | Q46851 |
| B | Aldo-keto reductase AKR14A1 | protein | 335 | 42% helix, 14% strand | Q46851 |
| C | Aldo-keto reductase AKR14A1 | protein | 330 | 41% helix, 14% strand | Q46851 |
| D | Aldo-keto reductase AKR14A1 | protein | 308 | 43% helix, 15% strand | Q46851 |
| E | Aldo-keto reductase AKR14A1 | protein | 297 | 41% helix, 16% strand | Q46851 |
| F | Aldo-keto reductase AKR14A1 | protein | 298 | 44% helix, 16% strand | Q46851 |
| G | Aldo-keto reductase AKR14A1 | protein | 335 | 43% helix, 14% strand | Q46851 |
| H | Aldo-keto reductase AKR14A1 | protein | 297 | 39% helix, 16% strand | Q46851 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 7 copies · chains A, B, C, E, F, G, H
- FLC · Citrate anion · additive · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 956 | 0.84 | 0.85 | 122 | empty |
| 2 | 969 | 0.83 | 0.84 | 125 | empty |
| 3 | 237 | 0.75 | 0.89 | 38 | NAP, FLC |
| 4 | 269 | 0.74 | 0.88 | 42 | NAP, FLC |
| 5 | 273 | 0.71 | 0.86 | 37 | NAP, FLC |
Interfaces
16 interfaces between chains.
- B–C · 946 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 944 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 941 Ų buried · 14 hydrogen bonds · protein-protein
- E–G · 941 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 933 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 4AUB · the complex Structure of the bacterial aldo-keto reductase AKR14A1 with NADP and citrate · the same entry in another collection · chain H against H, TM-score 1.00
- Q46851 · AlphaFold monomer V2.0 prediction for L-glyceraldehyde 3-phosphate reductase (Q46851) · a predicted model of the same protein · chain H 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 Q46851
- Elsewhere: RCSB PDB 4AUB · PDBe 4AUB · UniProt Q46851
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