CRYSTAL STRUCTURE OF NITRITE REDUCTASE HIS255ASN MUTANT FROM ALCALIGENES FAECALIS
The structure was published by Boulanger, M.J., Kukimoto, M., Nishiyama, M., Horinouchi, S., and Murphy, M.E., in 2000 in a paper entitled "Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2000.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of NITRITE REDUCTASE. This molecule has the UniProt identifier P38501 (NIR_ALCFA). The sample contained 341 residues which is 98% of the natural sequence. Out of 341 residues 339 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 molecule most likely forms homotrimers.
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):
This entry contains 1 unique UniProt protein: