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Crystal structure of Treponema pallidum TP0796 Flavin trafficking protein, a bifunctional FMN transferase/FAD pyrophosphatase, D284A mutant, ADN bound form
Analyse Crystal structure of Treponema pallidum TP0796 Flavin trafficking protein, a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XDR
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.4
- Source
- Treponema pallidum (strain Nichols)
- Molecule
- FAD:protein FMN transferase
- EC
- 2.7.1.180
- UniProt
- O83774
- Ligands
- ADN, MG
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · resolution 1.4 · 1 distinct chain · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD:protein FMN transferase (EC 2.7.1.180) | protein | 329 | 34% helix, 29% strand | O83774 |
Ligands and binding sites
- ADN · Adenosine · ligand · chains A
- MG · Magnesium ion · metal · chains A
- ACT · Acetate ion · additive · 6 copies · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · 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 | 406 | 0.73 | 0.83 | 44 | ADN, EDO |
| 2 | 211 | 0.49 | 0.75 | 27 | ACT |
| 3 | 92 | 0.40 | 0.77 | 18 | empty |
| 4 | 59 | 0.28 | 0.74 | 13 | empty |
| 5 | 51 | 0.27 | 0.74 | 12 | empty |
Compared structures
- 4XDR · Crystal structure of treponema pallidum TP0796 flavin trafficking protein, a bifunctional… · 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 O83774
- Elsewhere: RCSB PDB 4XDR · PDBe 4XDR · UniProt O83774
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