CRYSTAL STRUCTURE OF SOCS-4 IN COMPLEX WITH ELONGIN-B AND ELONGIN-C AT 2.55A RESOLUTION
The structure was published by Bullock, A.N., Rodriguez, M.C., Debreczeni, J.E., Songyang, Z., and Knapp, S., in 2007 in a paper entitled "Structure of the Socs4-Elonginb/C Complex Reveals a Distinct Socs Box Interface and the Molecular Basis for Socs-Dependent Egfr Degradation." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.55 Å and deposited in 2006.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 3 biomacromolecules, namely SUPPRESSOR OF CYTOKINE SIGNALING 4, TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2, and TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1.
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 heterotrimers.
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 3 unique UniProt proteins: