Research workbench
Fmnb complexed with ATP
Analyse Fmnb complexed with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ESB
- Type
- protein
- Length
- 316 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
- ATP, MG
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD:PROTEIN FMN transferase (EC 2.7.1.180) | protein | 316 | 32% helix, 27% strand | A0A0H3GJF7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 533 | 0.78 | 0.85 | 49 | ATP, MG |
| 2 | 106 | 0.41 | 0.76 | 20 | empty |
| 3 | 55 | 0.33 | 0.77 | 14 | empty |
Compared structures
- 7ESB · FmnB complexed with ATP · 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 7ESB · PDBe 7ESB · UniProt A0A0H3GJF7
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