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sc-PDB

An Annotated Database of Druggable Binding Sites from the Protein DataBank

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Distribution of Binding site similarity measured by Shaper
You can zoom onto the graph by using the mouse to make a selection

Binding Sites are compared using Shaper.
For more information, please see the following publication: Desaphy J. et al. Comparison and Druggability Prediction of protein-Ligand Binding sites from pharmacophore-annotated cavity shapes J. Chem. Inf. Model., 2012, 52(8), pp2287-2299
Binding Sites are considered as similar when the similarity value is greater than 0.44

Reference Protein Data Bank Entry :
PDB IDHETUniprot NameEC Number
1s64778Geranylgeranyl transferase type-1 subunit beta2.5.1.59

Complex with similar binding sites

PDB ID HET Uniprot Name EC Number Binding Site
Similarity		 Align
1s64778Geranylgeranyl transferase type-1 subunit beta2.5.1.591.000
1n4sCYS_VAL_ILE_LEU_GERGeranylgeranyl transferase type-1 subunit beta2.5.1.590.666
1n4qLYS_CYS_VAL_ILE_LEUGeranylgeranyl transferase type-1 subunit beta2.5.1.590.493
1mzcBNEProtein farnesyltransferase subunit beta2.5.1.580.490
1sa4JANProtein farnesyltransferase subunit beta2.5.1.580.489
1o1s1NHProtein farnesyltransferase subunit beta2.5.1.580.485
1n95FTHProtein farnesyltransferase subunit beta2.5.1.580.481
1ld8U49Protein farnesyltransferase subunit beta2.5.1.580.478
1n95HFPProtein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha/0.475
1n95HFPProtein farnesyltransferase subunit beta2.5.1.580.475
1s63778Protein farnesyltransferase subunit beta2.5.1.580.471
3e30ED4Protein farnesyltransferase subunit beta2.5.1.580.471
1nl4HFPProtein farnesyltransferase subunit beta2.5.1.580.470
3e33ED7Protein farnesyltransferase subunit beta2.5.1.580.465
3hxfBD9Geranylgeranyl transferase type-2 subunit beta2.5.1.600.465
1ld7U66Protein farnesyltransferase subunit beta2.5.1.580.463
1jcq739Protein farnesyltransferase subunit beta2.5.1.580.457
1sa5BMVProtein farnesyltransferase subunit beta2.5.1.580.456
3eu5GBOProtein farnesyltransferase subunit beta2.5.1.580.454