1hrk Summary



The structure was published by Wu, C.K., Dailey, H.A., Rose, J.P., Burden, A., Sellers, V.M., and Wang, B.C., in 2001 in a paper entitled "The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2000.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of FERROCHELATASE.

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 molecule most likely forms homodimers.

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 FERROCHELATASE P22830 (65-423) (HEMH_HUMAN)search Homo sapienssearch < 90% 359 100%
B FERROCHELATASE P22830 (65-423) (HEMH_HUMAN)search Homo sapienssearch < 90% 359 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P22830 (65 - 423) FERROCHELATASE Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Ferrochelatasesearch Rossmann foldsearch Ferrochelatasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P22830) ferrochelatase activitysearch heme biosynthetic processsearch

Chain InterPro annotation
A, B Ferrochelatasesearch Ferrochelatase, active sitesearch