MolNFT v1 · #9972 · protein
The structure of escherichia COLI nitroreductase complexed with nicotinic acid
1ICR · Oxygen-insensitive NAD(P)H nitroreductase: “The structure of escherichia COLI nitroreductase complexed with nicotinic acid”. X-ray diffraction, 2 ligands (FMN, NIO), 2 pockets (best druggability 0.76). MolNFT v1 #9972 on GenesisL1…
- PDB
- 1ICR
- Type
- protein
- Length
- 432 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, NIO
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Oxygen-insensitive NAD(P)H nitroreductase (EC 1.6.99.7) | protein | 216 | 55% helix, 15% strand | P38489 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- NIO · Nicotinic acid · 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 | 732 | 0.76 | 0.81 | 64 | FMN, NIO |
| 2 | 637 | 0.74 | 0.80 | 65 | NIO, FMN |
Interfaces
1 interface between chains.
- A–B · 3512 Ų buried · 58 hydrogen bonds · protein-protein
Compared structures
- 1ICR · The structure of escherichia COLI nitroreductase complexed with nicotinic acid · 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 1ICR · PDBe 1ICR · UniProt P38489
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.