MolNFT v1 · #74888 · protein
Crystal structure of phosphoribosylglycinamide formyltransferase from bacillus halodurans
3P9X: “Crystal structure of phosphoribosylglycinamide formyltransferase from bacillus halodurans”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.67). MolNFT v1 #74888 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3P9X
- Type
- protein
- Length
- 389 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosylglycinamide formyltransferase
- UniProt
- Q9KF54
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylglycinamide formyltransferase | protein | 195 | 37% helix, 21% strand | Q9KF54 |
| B | Phosphoribosylglycinamide formyltransferase | protein | 194 | 38% helix, 21% strand | Q9KF54 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 309 | 0.67 | 0.82 | 37 | SO4 |
| 2 | 329 | 0.66 | 0.81 | 38 | SO4, GOL |
| 3 | 52 | 0.24 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 523 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3P9X · Crystal structure of phosphoribosylglycinamide formyltransferase from Bacillus Halodurans · 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 Q9KF54
- Elsewhere: RCSB PDB 3P9X · PDBe 3P9X · UniProt Q9KF54
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