1fha Summary



The structure was published by Lawson, D.M., Artymiuk, P.J., Yewdall, S.J., et al., Thomas, C.D., Shaw, W.V., and Harrison, P.M., in 1991 in a paper entitled "Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 1990.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of FERRITIN. This molecule has the UniProt identifier P02794 (FRIH_HUMAN)search. The sample contained 183 residues which is 100% of the natural sequence. Out of 183 residues 163 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The most likely quaternary structure is a 24meric assembly.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A FERRITIN P02794 (1-183) (FRIH_HUMAN)search Homo sapienssearch 94% 183 93%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P02794 (1 - 183) FERRITIN Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P02794) Ferritinsearch Ferritin;search PF00210: Ferritin-like domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P02794) ferric iron bindingsearch protein bindingsearch iron ion bindingsearch ferroxidase activitysearch oxidoreductase activitysearch metal ion bindingsearch immune responsesearch post-Golgi vesicle-mediated transportsearch iron ion transportsearch cellular iron ion homeostasissearch receptor-mediated endocytosissearch negative regulation of cell proliferationsearch membrane organizationsearch transmembrane transportsearch oxidation-reduction processsearch intracellular sequestering of iron ionsearch negative regulation of fibroblast proliferationsearch cytosolsearch nucleussearch extracellular exosomesearch mitochondrionsearch intracellular ferritin complexsearch

Chain InterPro annotation
A Ferritinsearch Ferritin/DPS protein domainsearch Ferritin- like diiron domainsearch Ferritin-like superfamilysearch Ferritin-relatedsearch Ferritin, conserved sitesearch