1fgj Summary

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X-RAY STRUCTURE OF HYDROXYLAMINE OXIDOREDUCTASE

The structure was published by Igarashi, N., Moriyama, H., Fujiwara, T., Fukumori, Y., and Tanaka, N., in 1997 in a paper entitled "The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 1997.

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

This PDB entry contains multiple copies of the structure of HYDROXYLAMINE OXIDOREDUCTASE.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 HYDROXYLAMINE OXIDOREDUCTASE Q50925 (25-570) (HAO_NITEU)search Nitrosomonas europaea ATCC 19718search 100% 546 91%
B HYDROXYLAMINE OXIDOREDUCTASE Q50925 (25-570) (HAO_NITEU)search Nitrosomonas europaea ATCC 19718search 100% 546 91%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q50925 (25 - 570) HYDROXYLAMINE OXIDOREDUCTASE Nitrosomonas europaea

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (Q50925) Di-heme elbow motifsearch Hydroxylamine Oxidoreductase; Chain A, domain 1search, Hydroxylamine Oxidoreductase; Chain A, domain 2search PF13447: Seven times multi-haem cytochrome CxxCHsearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A, B (Q50925) periplasmic spacesearch oxidoreductase activitysearch metal ion bindingsearch oxidation-reduction processsearch anaerobic respiration, using ammonium as electron donorsearch

Chain InterPro annotation
A, B Multihaem cytochromesearch Hydroxylamine oxidasesearch