1FQF
CRYSTAL STRUCTURES OF MUTANT (K296A) 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) | water | water | 18.0 | 278 | Chemie (HOH) |
Sequence modifications
A: 1 - 331 (UniProt: P02787)
| PDB | External Database | Details |
|---|---|---|
| Ala 296 | Lys 315 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 36546.6 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 115.9 | |
| All* | Total formula weight | 36662.4 |
