1FQE
CRYSTAL STRUCTURES OF MUTANT (K206A) THAT ABOLISH THE DILYSINE INTERACTION IN THE N-LOBE OF HUMAN TRANSFERRIN
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A (A) | SEROTRANSFERRIN | polymer | 331 | 36546.6 | 1 | UniProt (P02787) Pfam (PF00405) | Homo sapiens (human) | SERUM TRANSFERRIN |
2 | B (A) | FE (III) ION | non-polymer | 55.8 | 1 | Chemie (FE) | |||
3 | C (A) | CARBONATE ION | non-polymer | 60.0 | 1 | Chemie (CO3) | |||
4 | D (A) | POTASSIUM ION | non-polymer | 39.1 | 1 | Chemie (K) | |||
5 | E (A) | water | water | 18.0 | 442 | Chemie (HOH) |
Sequence modifications
A: 1 - 331 (UniProt: P02787)
PDB | External Database | Details |
---|---|---|
Ala 206 | Lys 225 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 36546.6 | |
Non-Polymers* | Number of molecules | 3 |
Total formula weight | 155.0 | |
All* | Total formula weight | 36701.5 |