MolNFT v1 · #177733 · protein
The complex structure of flavin transferase fmnb complexed with FAD
7ESA · FAD:PROTEIN FMN transferase: “The complex structure of flavin transferase fmnb complexed with FAD”. X-ray diffraction, 2 ligands (FAD, MG), 2 pockets (best druggability 0.79). MolNFT v1 #177733 on GenesisL1: 3D structure, binding…
- PDB
- 7ESA
- Type
- protein
- Length
- 322 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAD:PROTEIN FMN transferase
- EC
- 2.7.1.180
- UniProt
- A0A0H3GJF7
- Ligands
- FAD, MG
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD:PROTEIN FMN transferase (EC 2.7.1.180) | protein | 322 | 30% helix, 26% strand | A0A0H3GJF7 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 585 | 0.79 | 0.85 | 65 | FAD, MG |
| 2 | 129 | 0.46 | 0.77 | 23 | empty |
Compared structures
- 7ESA · the complex structure of flavin transferase FmnB complexed with FAD · 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 A0A0H3GJF7
- Elsewhere: RCSB PDB 7ESA · PDBe 7ESA · UniProt A0A0H3GJF7
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