MolNFT v1 · #84557 · protein
Crystal structure of FMN-binding protein (YP_005476) from thermus thermophilus with bound benzene-1,4-diol
3ZOF · Flavoredoxin: “Crystal structure of FMN-binding protein (YP_005476) from thermus thermophilus with bound benzene-1,4-diol”. X-ray diffraction, 2 ligands (HQE, FMN), 3 pockets (best druggability 0.77). MolNFT v1 #84557 on GenesisL1…
- PDB
- 3ZOF
- Type
- protein
- Length
- 356 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavoredoxin
- UniProt
- Q72HI0
- Ligands
- HQE, FMN
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Flavoredoxin | protein | 178 | 13% helix, 46% strand | Q72HI0 |
Ligands and binding sites
- HQE · benzene-1,4-diol · ligand · 2 copies · chains A, B
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.77 | 0.99 | 21 | empty |
| 2 | 301 | 0.61 | 0.79 | 40 | HQE, FMN |
| 3 | 282 | 0.60 | 0.79 | 38 | HQE, FMN |
Interfaces
1 interface between chains.
- A–B · 3834 Ų buried · 44 hydrogen bonds · protein-protein
Compared structures
- 3ZOF · Crystal structure of FMN-binding protein (YP_005476) from Thermus thermophilus with bound… · the same entry in another collection · 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 Q72HI0
- Elsewhere: RCSB PDB 3ZOF · PDBe 3ZOF · UniProt Q72HI0
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