Research workbench
X-ray structure of the fdtf N-formyltransferase from salmonella enteric O60 in complex with tdp
Analyse X-ray structure of the fdtf N-formyltransferase from salmonella enteric O60 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UIJ
- Type
- protein
- Length
- 795 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Formyltransferase
- UniProt
- U3GK13
- Ligands
- TYD, NA
- Pockets
- 7 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Formyltransferase | protein | 398 | 36% helix, 18% strand | U3GK13 |
| B | Formyltransferase | protein | 397 | 36% helix, 18% strand | U3GK13 |
Ligands and binding sites
- TYD · Thymidine-5'-diphosphate · ligand · 4 copies · chains A, B
- NA · Sodium ion · metal · 5 copies · chains A, B
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 668 | 0.74 | 0.80 | 65 | TYD |
| 2 | 633 | 0.72 | 0.79 | 62 | TYD |
| 3 | 719 | 0.71 | 0.77 | 52 | empty |
| 4 | 382 | 0.58 | 0.76 | 44 | empty |
| 5 | 370 | 0.58 | 0.76 | 45 | empty |
Interfaces
1 interface between chains.
- A–B · 1321 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 5UIJ · X-ray structure of The FdtF N-formyltransferase from Salmonella enteric O60 in complex… · the same entry in another collection · chain B against B, 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 U3GK13
- Elsewhere: RCSB PDB 5UIJ · PDBe 5UIJ · UniProt U3GK13
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