Structural highlights
5n26 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , |
| Gene: | FTH1, FTH, FTHL6, OK/SW-cl.84, PIG15 (HUMAN) |
| Activity: | Ferroxidase, with EC number 1.16.3.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[FRIH_HUMAN] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
Publication Abstract from PubMed
The aim of this work is to identify the cisplatin binding sites on human H-chain ferritin. High-resolution X-ray crystallography reveals that cisplatin binds four distinct protein sites, that is, the side chains of His136 and Lys68, the side chain of His105, the side chain of Cys90 and the side chain of Cys102. These Pt binding sites are compared with those observed for the adduct that cisplatin forms upon encapsulation within horse spleen L-chain ferritin (87% identity with human L-chain ferritin).
Cisplatin Binding Sites in Human H-Chain Ferritin.,Ferraro G, Ciambellotti S, Messori L, Merlino A Inorg Chem. 2017 Jul 24. doi: 10.1021/acs.inorgchem.7b01072. PMID:28737381[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ferraro G, Ciambellotti S, Messori L, Merlino A. Cisplatin Binding Sites in Human H-Chain Ferritin. Inorg Chem. 2017 Jul 24. doi: 10.1021/acs.inorgchem.7b01072. PMID:28737381 doi:http://dx.doi.org/10.1021/acs.inorgchem.7b01072
