1ksu Summary


Crystal Structure of His505Tyr Mutant Flavocytochrome c3 from Shewanella frigidimarina

The structure was published by Pankhurst, K.L., Mowat, C.G., Miles, C.S., et al., Walkinshaw, M.D., Reid, G.A., and Chapman, S.K., in 2002 in a paper entitled "Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2002.

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

This PDB entry contains multiple copies of the structure of flavocytochrome c.

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 flavocytochrome c P0C278 (1-571) (FRDA_SHEFR)search Shewanella frigidimarinasearch 100% 571 99%
B flavocytochrome c P0C278 (1-571) (FRDA_SHEFR)search Shewanella frigidimarinasearch 100% 571 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0C278 (1 - 571) flavocytochrome c Shewanella frigidimarina

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P0C278) Di-heme elbow motifsearch, Succinate dehydrogenase/fumarate reductase flavoprotein N-terminal domainsearch, Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domainsearch Flavocytochrome C3; Chain A, domain 1search, Flavocytochrome C3; Chain Asearch, FAD/NAD(P)-binding domainsearch PF00890: FAD binding domainsearch, PF14537: Cytochrome c3search

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A, B (P0C278) metal ion bindingsearch succinate dehydrogenase activitysearch electron carrier activitysearch oxidoreductase activitysearch periplasmic spacesearch outer membrane-bounded periplasmic spacesearch oxidation-reduction processsearch anaerobic electron transport chainsearch anaerobic respirationsearch

Chain InterPro annotation
A, B FAD binding domainsearch Zinc finger, C2H2search Flavocytochrome csearch Multihaem cytochromesearch Tetrahaem cytochrome domainsearch FAD-dependent pyridine nucleotide-disulphide oxidoreductasesearch Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domainsearch