1ged Summary


A positive charge route for the access of nadh to heme formed in the distal heme pocket of cytochrome p450nor

The structure was published by Kudo, T., Takaya, N., Park, S.-Y., Shiro, Y., and Shoun, H., in 2001 in a paper entitled "A positively charged cluster formed in the heme-distal pocket of cytochrome P450nor is essential for interaction with NADH" (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 not deposited.

The PDB entry contains the structure of CYTOCHROME P450 55A1. This molecule has the UniProt identifier P23295 (NOR_FUSOX)search. The sample contained 403 residues which is 100% of the natural sequence. Out of 403 residues 399 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 is most likely monomeric.

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 CYTOCHROME P450 55A1 P23295 (1-403) (NOR_FUSOX)search Fusarium oxysporumsearch 100% 403 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P23295 (1 - 403) CYTOCHROME P450 55A1 Fusarium oxysporum

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P23295) Cytochrome P450search Cytochrome p450search PF00067: Cytochrome P450search

Chain ID Molecular function (GO) Biological process (GO)
A (P23295) oxidoreductase activitysearch iron ion bindingsearch heme bindingsearch oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygensearch metal ion bindingsearch monooxygenase activitysearch oxidation-reduction processsearch

Chain InterPro annotation
A Cytochrome P450search Cytochrome P450, B-classsearch Cytochrome P450, conserved sitesearch