5EHV
human carbonic anhydrase II in complex with ligand
Summary for 5EHV
| Entry DOI | 10.2210/pdb5ehv/pdb |
| Related | 5EH5 5EH7 5EH8 5EHW 5FLO 5FLP 5FLQ 5FLR 5FLS 5FLT 5FNG 5FNH 5FNI 5FNJ 5FNK 5FNM |
| Descriptor | Carbonic anhydrase 2, (~{E})-3-[3-[[3-(2-hydroxy-2-oxoethyl)phenyl]methoxy]phenyl]prop-2-enoic acid, ZINC ION, ... (7 entities in total) |
| Functional Keywords | human carbonic anhydrase ii, transferase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm : P00918 |
| Total number of polymer chains | 1 |
| Total formula weight | 29827.90 |
| Authors | |
| Primary citation | Woods, L.A.,Dolezal, O.,Ren, B.,Ryan, J.H.,Peat, T.S.,Poulsen, S.A. Native State Mass Spectrometry, Surface Plasmon Resonance, and X-ray Crystallography Correlate Strongly as a Fragment Screening Combination. J.Med.Chem., 59:2192-2204, 2016 Cited by PubMed Abstract: Fragment-based drug discovery (FBDD) is contingent on the development of analytical methods to identify weak protein-fragment noncovalent interactions. Herein we have combined an underutilized fragment screening method, native state mass spectrometry, together with two proven and popular fragment screening methods, surface plasmon resonance and X-ray crystallography, in a fragment screening campaign against human carbonic anhydrase II (CA II). In an initial fragment screen against a 720-member fragment library (the "CSIRO Fragment Library") seven CA II binding fragments, including a selection of nonclassical CA II binding chemotypes, were identified. A further 70 compounds that comprised the initial hit chemotypes were subsequently sourced from the full CSIRO compound collection and screened. The fragment results were extremely well correlated across the three methods. Our findings demonstrate that there is a tremendous opportunity to apply native state mass spectrometry as a complementary fragment screening method to accelerate drug discovery. PubMed: 26882437DOI: 10.1021/acs.jmedchem.5b01940 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.208 Å) |
Structure validation
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