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sc-PDB

An Annotated Database of Druggable Binding Sites from the Protein DataBank

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Distribution of Cavity similarities measured by Shaper
You can zoom onto the graph by using the mouse to make a selection

Cavities 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

Reference Protein Data Bank Entry :
PDB ID HET Uniprot Name EC Number
1tdcUMPThymidylate synthase

Complex with similar cavities

PDB ID HET Uniprot Name EC Number Cavity
Similarity
Align
1tdcUMPThymidylate synthase/1.000
1bp0UMPThymidylate synthase/0.641
2g8dUMPThymidylate synthase/0.625
1thyUMPThymidylate synthase/0.615
1njcDCMThymidylate synthase/0.590
1jmiUMPThymidylate synthase/0.581
1njaDCMThymidylate synthase/0.581
2g89UMPThymidylate synthase/0.575
1jmhUMPThymidylate synthase/0.572
1vzaUMPThymidylate synthase/0.560
1jmgUMPThymidylate synthase/0.558
1tsyUMPThymidylate synthase/0.551
1bp6UMPThymidylate synthase/0.543
2tdmUMPThymidylate synthase/0.542
4dpdUMPBifunctional dihydrofolate reductase-thymidylate synthase/0.539
3dg8UMPBifunctional dihydrofolate reductase-thymidylate synthase1.5.1.30.537
2g86UMPThymidylate synthase/0.523
1njeDCMThymidylate synthase/0.519
1tsxUMPThymidylate synthase/0.503
2vf0F89Thymidylate synthase/0.501
1tsvUMPThymidylate synthase/0.499
3dgaUMPBifunctional dihydrofolate reductase-thymidylate synthase1.5.1.30.495
4e5oUMPThymidylate synthase2.1.1.450.493
4dq1UMPThymidylate synthase/0.486
4eb4UMPThymidylate synthase2.1.1.450.485
1j3jUMPBifunctional dihydrofolate reductase-thymidylate synthase1.5.1.30.481
1njbUMPThymidylate synthase/0.467
4h0uUMPThymidylate synthase/0.463
1bidUMPThymidylate synthase/0.461
4fogC2FThymidylate synthase ThyA/0.461
1f4eTPRThymidylate synthase/0.460
1njdUMPThymidylate synthase/0.458
1vzbUMPThymidylate synthase/0.455
1f28UMPThymidylate synthase2.1.1.450.450
3qj7UMPThymidylate synthase ThyA/0.450