MolNFT v1 · #129118 · protein
Crystal structure of aspergillus fumigatus N-acetylphosphoglucosamine mutase in complex with glcnac-6P and magnesium
5OAW · Phosphoacetylglucosamine mutase: “Crystal structure of aspergillus fumigatus N-acetylphosphoglucosamine mutase in complex with glcnac-6P and…”. X-ray diffraction, 2 ligands (16G, MG), 11 pockets (best druggability 0.78). MolNFT v1…
- PDB
- 5OAW
- Type
- protein
- Length
- 1,033 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoacetylglucosamine mutase
- EC
- 5.4.2.3
- UniProt
- A0A0S7E9S6
- Ligands
- 16G, MG
- Pockets
- 11 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoacetylglucosamine mutase (EC 5.4.2.3) | protein | 534 | 41% helix, 19% strand | A0A0S7E9S6 |
| B | Phosphoacetylglucosamine mutase (EC 5.4.2.3) | protein | 499 | 42% helix, 18% strand | A0A0S7E9S6 |
Ligands and binding sites
- 16G · 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · 3 copies · chains A, B
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 | 1131 | 0.78 | 0.80 | 99 | 16G |
| 2 | 598 | 0.69 | 0.78 | 81 | GOL |
| 3 | 444 | 0.64 | 0.78 | 36 | 16G, GOL |
| 4 | 112 | 0.62 | 0.87 | 23 | empty |
| 5 | 491 | 0.62 | 0.75 | 66 | empty |
Interfaces
1 interface between chains.
- A–B · 593 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 5OAW · Crystal structure of Aspergillus fumigatus N-acetylphosphoglucosamine mutase in complex… · 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 A0A0S7E9S6
- Elsewhere: RCSB PDB 5OAW · PDBe 5OAW · UniProt A0A0S7E9S6
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