1zhi Summary


Complex of the S. cerevisiae Orc1 and Sir1 interacting domains

The structure was published by Hou, Z., Bernstein, D.A., Fox, C.A., and Keck, J.L., in 2005 in a paper entitled "Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2005.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely Origin recognition complex subunit 1 and Regulatory protein SIR1.

The molecule most likely forms heterodimers.

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 Origin recognition complex subunit 1 P54784 (1-219) (ORC1_YEAST)search Saccharomyces cerevisiae S288csearch < 90% 225 86%
B Regulatory protein SIR1 P21691 (456-587) (SIR1_YEAST)search Saccharomyces cerevisiae S288csearch < 90% 138 90%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P54784 (1 - 219) Origin recognition complex subunit 1 Saccharomyces cerevisiae
P21691 (456 - 587) Regulatory protein SIR1 Saccharomyces cerevisiae

Chain Structural classification (SCOP) Sequence family (Pfam)
A BAH domainsearch BAH domainsearch
B ORC1-binding domainsearch Regulatory protein Sir1search

Chain ID Molecular function (GO)
A (P54784) DNA bindingsearch

Chain InterPro annotation
A Bromo adjacent homology (BAH) domainsearch
B Regulatory protein Sir1search