4ibc Summary

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Ebola virus VP35 bound to small molecule

The structure was published by Brown, C.S., Lee, M.S., Leung, D.W., et al., Ready, J.M., Basler, C.F., and Amarasinghe, G.K., in 2014 in a paper entitled "In Silico Derived Small Molecules Bind the Filovirus VP35 Protein and Inhibit Its Polymerase Cofactor Activity." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.745 Å and deposited in 2012.

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

This PDB entry contains multiple copies of the structure of Polymerase cofactor VP35.

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 Polymerase cofactor VP35 Q05127 (215-340) (VP35_EBOZM)search Ebola virus - Mayinga, Zaire, 1976search < 90% 129 95%
B Polymerase cofactor VP35 Q05127 (215-340) (VP35_EBOZM)search Ebola virus - Mayinga, Zaire, 1976search < 90% 129 95%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q05127 (215 - 340) Polymerase cofactor VP35 Ebola virus - Mayinga, Zaire, 1976

Chain Sequence family (Pfam)
A, B Filoviridae VP35search
Chain InterPro annotation
A, B Filoviridae VP35 proteinsearch