MolNFT v1 · #17292 · protein
Nitroreductase from E-COLI in complex with the inhibitor dicoumarol
1OOQ · Oxygen-insensitive NAD(P)H nitroreductase: “Nitroreductase from E-COLI in complex with the inhibitor dicoumarol”. X-ray diffraction, 2 ligands (FMN, DTC), 4 pockets (best druggability 0.75). MolNFT v1 #17292 on GenesisL1: 3D…
- PDB
- 1OOQ
- Type
- protein
- Length
- 433 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxygen-insensitive NAD(P)H nitroreductase
- EC
- 1.6.99.7
- UniProt
- P38489
- Ligands
- FMN, DTC
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxygen-insensitive NAD(P)H nitroreductase (EC 1.6.99.7) | protein | 217 | 53% helix, 15% strand | P38489 |
| B | Oxygen-insensitive NAD(P)H nitroreductase (EC 1.6.99.7) | protein | 216 | 53% helix, 15% strand | P38489 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- DTC · Bishydroxy[2h-1-benzopyran-2-one,1,2-benzopyrone] · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 467 | 0.75 | 0.83 | 41 | FMN, DTC |
| 2 | 478 | 0.73 | 0.82 | 43 | FMN |
| 3 | 202 | 0.52 | 0.77 | 25 | empty |
| 4 | 203 | 0.52 | 0.77 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 3717 Ų buried · 56 hydrogen bonds · protein-protein
Compared structures
- 1OOQ · Nitroreductase from e-coli in complex with the inhibitor dicoumarol · the same entry in another collection · chain A against A, TM-score 1.00
- P38489 · AlphaFold monomer V2.0 prediction for oxygen-insensitive NAD(P)H nitroreductase (P38489) · a predicted model of the same protein · chain A 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 P38489
- Elsewhere: RCSB PDB 1OOQ · PDBe 1OOQ · UniProt P38489
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