Research workbench
Genetic and structural validation of aspergillus fumigatus N-acetylphosphoglucosamine mutase as an antifungal target
Analyse Genetic and structural validation of aspergillus fumigatus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BJU
- Type
- protein
- Length
- 1,090 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetylglucosamine-phosphate mutase
- EC
- 5.4.2.3
- UniProt
- B0XPI4
- Ligands
- MG
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylglucosamine-phosphate mutase (EC 5.4.2.3) | protein | 548 | 42% helix, 18% strand | B0XPI4 |
| B | N-acetylglucosamine-phosphate mutase (EC 5.4.2.3) | protein | 542 | 43% helix, 19% strand | B0XPI4 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 965 | 0.74 | 0.77 | 96 | empty |
| 2 | 830 | 0.73 | 0.78 | 69 | empty |
| 3 | 852 | 0.71 | 0.76 | 92 | empty |
| 4 | 208 | 0.62 | 0.82 | 24 | empty |
| 5 | 162 | 0.45 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 564 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 4BJU · Genetic and structural validation of Aspergillus fumigatus N- acetylphosphoglucosamine… · 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 B0XPI4
- Elsewhere: RCSB PDB 4BJU · PDBe 4BJU · UniProt B0XPI4
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