1SZX
Role Of Hydrogen Bonding In The Active Site Of Human Manganese Superoxide Dismutase
Replaces: 1RFWEntity
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) | Superoxide dismutase [Mn], mitochondrial | polymer | 198 | 22178.1 | 2 | UniProt (P04179) Pfam (PF00081) Pfam (PF02777) | Homo sapiens (human) | |
2 | C, D (A, B) | MANGANESE (II) ION | non-polymer | 54.9 | 2 | Chemie (MN) | |||
3 | E, F (A, B) | water | water | 18.0 | 418 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 198 (UniProt: P04179)
PDB | External Database | Details |
---|---|---|
Phe 34 | Tyr 58 | engineered mutation |
Phe 123 | Trp 147 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 44356.2 | |
Non-Polymers* | Number of molecules | 2 |
Total formula weight | 109.9 | |
All* | Total formula weight | 44466.0 |