1JRQ
X-ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. coli Amine Oxidase
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) | Copper amine oxidase | polymer | 727 | 81350.7 | 2 | UniProt (P46883) Pfam (PF07833) Pfam (PF02727) Pfam (PF02728) Pfam (PF01179) | Escherichia coli | TYRAMINE OXIDASE, 2-PHENYLENTHYLAMINE OXIDASE |
2 | C, F (A, B) | COPPER (II) ION | non-polymer | 63.5 | 2 | Chemie (CU) | |||
3 | D, E, G, H (A, B) | CALCIUM ION | non-polymer | 40.1 | 4 | Chemie (CA) | |||
4 | I, J (A, B) | water | water | 18.0 | 1394 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 727 (UniProt: P46883)
PDB | External Database | Details |
---|---|---|
Phe 369 | Tyr 399 | engineered mutation |
Tpq 466 | Tyr 496 | modified residue |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 162701.5 | |
Non-Polymers* | Number of molecules | 6 |
Total formula weight | 287.4 | |
All* | Total formula weight | 162988.9 |