Research workbench
A unique GCN5-related glucosamine N-acetyltransferase region exist in the fungal multi-domain GH3 beta-N-acetylglucosaminidase
Analyse A unique GCN5-related glucosamine N-acetyltransferase region exist in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZM6
- Type
- protein
- Length
- 1,688 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyl-beta-D glucosaminidase
- EC
- 3.2.1.52, 2.3.1.3
- UniProt
- V9M3A9
- Ligands
- ACO, SO4
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | N-acetyl-beta-D glucosaminidase (EC 3.2.1.52, 2.3.1.3) | protein | 844 | 39% helix, 19% strand | V9M3A9 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1176 | 0.78 | 0.80 | 113 | ACO |
| 2 | 953 | 0.76 | 0.79 | 69 | empty |
| 3 | 265 | 0.70 | 0.85 | 33 | ACO |
| 4 | 410 | 0.66 | 0.79 | 65 | SO4 |
| 5 | 436 | 0.65 | 0.78 | 60 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1091 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 4ZM6 · A unique GCN5-related glucosamine N-acetyltransferase region exist in the fungal… · 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 V9M3A9
- Elsewhere: RCSB PDB 4ZM6 · PDBe 4ZM6 · UniProt V9M3A9
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