4R4Y
Structural basis of a point mutation that causes the genetic disease Aspartylglucosaminuria
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase | polymer | 295 | 32237.7 | 2 | UniProt (Q47898) Pfam (PF01112) | Elizabethkingia miricola | Aspartylglucosaminidase, AGA, Glycosylasparaginase, N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase, Glycosylasparaginase alpha chain, Glycosylasparaginase beta chain |
| 2 | C (A) | N-hydroxy-L-asparagine | non-polymer | 148.1 | 1 | Chemie (SD4) | |||
| 3 | D, E (A, B) | water | water | 18.0 | 87 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 295 (UniProt: Q47898)
| PDB | External Database | Details |
|---|---|---|
| Asp 172 | Gly 217 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 64475.3 | |
| Non-Polymers* | Number of molecules | 1 |
| Total formula weight | 148.1 | |
| All* | Total formula weight | 64623.5 |
