MolNFT v1 · #125850 · protein
Flavodiiron core of escherichia COLI flavorubredoxin in the reduced form.
5LLD · Anaerobic nitric oxide reductase flavorubredoxin: “Flavodiiron core of escherichia COLI flavorubredoxin in the reduced form.”. X-ray diffraction, 3 ligands (FMN, FE, OXY), 5 pockets (best druggability 0.68). MolNFT v1 #125850 on…
- PDB
- 5LLD
- Type
- protein
- Length
- 398 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anaerobic nitric oxide reductase flavorubredoxin
- UniProt
- Q46877
- Ligands
- FMN, FE, OXY
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anaerobic nitric oxide reductase flavorubredoxin | protein | 398 | 37% helix, 23% strand | Q46877 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- FE · Fe (III) ion · metal · 2 copies · chains A
- OXY · Oxygen molecule · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.68 | 0.90 | 30 | empty |
| 2 | 60 | 0.38 | 0.80 | 18 | FMN |
| 3 | 51 | 0.36 | 0.80 | 21 | OXY |
| 4 | 63 | 0.30 | 0.74 | 13 | empty |
| 5 | 53 | 0.29 | 0.75 | 12 | empty |
Compared structures
- 5LLD · Flavodiiron core of Escherichia coli flavorubredoxin in the reduced form. · the same entry in another collection · chain A against A, TM-score 1.00
- Q46877 · AlphaFold monomer V2.0 prediction for anaerobic nitric oxide reductase flavorubredoxin… · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q46877
- Elsewhere: RCSB PDB 5LLD · PDBe 5LLD · UniProt Q46877
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