MolNFT v1 · #6316 · protein
Crystal structure of NADH peroxidase mutant: R303M
1F8W: “Crystal structure of NADH peroxidase mutant: R303M”. X-ray diffraction, 1 ligand (FAD), 2 pockets (best druggability 0.79). MolNFT v1 #6316 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1F8W
- Type
- protein
- Length
- 447 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADH peroxidase
- EC
- 1.11.1.1
- UniProt
- P37062
- Ligands
- FAD
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH peroxidase (EC 1.11.1.1) | protein | 447 | 26% helix, 30% strand | P37062 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
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 | 1142 | 0.79 | 0.80 | 98 | FAD |
| 2 | 82 | 0.53 | 0.85 | 22 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
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 P37062
- Elsewhere: RCSB PDB 1F8W · PDBe 1F8W · UniProt P37062
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.