1ezv Summary

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STRUCTURE OF THE YEAST CYTOCHROME BC1 COMPLEX CO-CRYSTALLIZED WITH AN ANTIBODY FV-FRAGMENT

The structure was published by Hunte, C., Koepke, J., Lange, C., Rossmanith, T., and Michel, H., in 2000 in a paper entitled "Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2000.

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

This entry contains 28 copies of 11 unique biopolymers (complete list).

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 most likely quaternary structure is a 20meric assembly.


The are more than 5 unique protein polymers in this entry. More information is available on the Uniprot cross references page.

This entry contains 11 unique UniProt proteins:

UniProt accession Name Organism PDB
P07256 (27 - 457) UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I Saccharomyces cerevisiae
P07257 (17 - 368) UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2 Saccharomyces cerevisiae
P00163 (1 - 385) CYTOCHROME B Saccharomyces cerevisiae
P07143 (62 - 306) CYTOCHROME C1 Saccharomyces cerevisiae
P08067 (31 - 215) UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT Saccharomyces cerevisiae
P00127 (74 - 147) UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 17 KD PROTEIN Saccharomyces cerevisiae
P00128 (3 - 127) UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN Saccharomyces cerevisiae
P08525 (2 - 94) UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C Saccharomyces cerevisiae
P22289 (4 - 58) UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.3 KD PROTEIN Saccharomyces cerevisiae
P18531 (20 - 116) HEAVY CHAIN (VH) OF FV-FRAGMENT Mus musculus
P01647 (10 - 107) LIGHT CHAIN (VL) OF FV-FRAGMENT Mus musculus

For more information on cross references to other databases click Cross references in the menu on the left.