MolNFT v1 · #166856 · protein
X-ray structure of a sugar N-formyltransferase from pseudomonas congelans
6V33 · Dtdp-4-amino-4,6-dideoxyglucose formyltransferase: “X-ray structure of a sugar N-formyltransferase from pseudomonas congelans”. X-ray diffraction, 2 ligands (0FX, FOL), 4 pockets (best druggability 0.72). MolNFT v1 #166856 on…
- PDB
- 6V33
- Type
- protein
- Length
- 491 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dtdp-4-amino-4,6-dideoxyglucose formyltransferase
- UniProt
- A0A0N8R1B2
- Ligands
- 0FX, FOL
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dtdp-4-amino-4,6-dideoxyglucose formyltransferase | protein | 246 | 35% helix, 26% strand | A0A0N8R1B2 |
| B | Dtdp-4-amino-4,6-dideoxyglucose formyltransferase | protein | 245 | 33% helix, 27% strand | A0A0N8R1B2 |
Ligands and binding sites
- 0FX · dTDP-4-amino-4,6-dideoxyglucose · ligand · 2 copies · chains A, B
- FOL · Folic acid · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 456 | 0.72 | 0.81 | 43 | 0FX, FOL |
| 2 | 426 | 0.72 | 0.82 | 43 | 0FX, FOL |
| 3 | 83 | 0.38 | 0.77 | 20 | EDO |
| 4 | 74 | 0.34 | 0.76 | 21 | EDO |
Interfaces
1 interface between chains.
- A–B · 1611 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 6V33 · X-ray structure of a sugar N-formyltransferase from Pseudomonas congelans · 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 A0A0N8R1B2
- Elsewhere: RCSB PDB 6V33 · PDBe 6V33 · UniProt A0A0N8R1B2
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