Research workbench
Structural of aspergillus fumigatus udp-N-acetylglucosamine pyrophosphorylase
Analyse Structural of aspergillus fumigatus udp-N-acetylglucosamine pyrophosphorylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BMA
- Type
- protein
- Length
- 912 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine pyrophosphorylase
- EC
- 2.7.7.23
- UniProt
- Q4WAR0
- Pockets
- 11 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) | protein | 465 | 41% helix, 22% strand | Q4WAR0 |
| B | Udp-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) | protein | 447 | 40% helix, 23% strand | Q4WAR0 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 775 | 0.70 | 0.76 | 67 | GOL |
| 2 | 610 | 0.69 | 0.78 | 48 | empty |
| 3 | 167 | 0.62 | 0.84 | 25 | empty |
| 4 | 216 | 0.59 | 0.81 | 28 | empty |
| 5 | 225 | 0.57 | 0.79 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 662 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4BMA · structural of Aspergillus fumigatus UDP-N-acetylglucosamine pyrophosphorylase · 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 Q4WAR0
- Elsewhere: RCSB PDB 4BMA · PDBe 4BMA · UniProt Q4WAR0
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