MolNFT v1 · #50421 · protein
P94L actinorhodin ketordeuctase mutant, with NADPH and inhibitor emodin
2RHR · Actinorhodin polyketide ketoreductase: “P94L actinorhodin ketordeuctase mutant, with NADPH and inhibitor emodin”. X-ray diffraction, 2 ligands (NDP, EMO), 4 pockets (best druggability 0.76). MolNFT v1 #50421 on GenesisL1: 3D…
- PDB
- 2RHR
- Type
- protein
- Length
- 512 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actinorhodin polyketide ketoreductase
- EC
- 1.3.1.-
- UniProt
- P16544
- Ligands
- NDP, EMO
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Actinorhodin polyketide ketoreductase (EC 1.3.1.-) | protein | 256 | 46% helix, 16% strand | P16544 |
| A | Actinorhodin polyketide ketoreductase (EC 1.3.1.-) | protein | 256 | 49% helix, 16% strand | P16544 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains B, A
- EMO · 3-methyl-1,6,8-trihydroxyanthraquinone · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 734 | 0.76 | 0.81 | 61 | NDP, EMO |
| 2 | 586 | 0.74 | 0.81 | 56 | NDP |
| 3 | 131 | 0.45 | 0.77 | 30 | empty |
| 4 | 74 | 0.37 | 0.78 | 12 | empty |
Interfaces
1 interface between chains.
- B–A · 1651 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 2RHR · P94L actinorhodin ketordeuctase mutant, with NADPH and Inhibitor Emodin · the same entry in another collection · chain B against B, TM-score 1.00
- P16544 · AlphaFold monomer V2.0 prediction for putative ketoacyl reductase (P16544) · a predicted model of the same protein · chain B 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 P16544
- Elsewhere: RCSB PDB 2RHR · PDBe 2RHR · UniProt P16544
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