5KGN
1.95A resolution structure of independent phosphoglycerate mutase from C. elegans in complex with a macrocyclic peptide inhibitor (2d)
Summary for 5KGN
Entry DOI | 10.2210/pdb5kgn/pdb |
Related | 5KGL 5KGM |
Descriptor | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, macrocyclic peptide inhibitor, CHLORIDE ION, ... (8 entities in total) |
Functional Keywords | metal binding, coupled enzyme assay, hts, structure activity relationship, rapid systems, high throughput enzymology, isomerase |
Biological source | Caenorhabditis elegans More |
Total number of polymer chains | 4 |
Total formula weight | 120870.56 |
Authors | Lovell, S.,Mehzabeen, N.,Battaile, K.P.,Yu, H.,Dranchak, P.,MacArthur, R.,Li, Z.,Carlow, T.,Suga, H.,Inglese, J. (deposition date: 2016-06-13, release date: 2017-04-05, Last modification date: 2023-09-27) |
Primary citation | Yu, H.,Dranchak, P.,Li, Z.,MacArthur, R.,Munson, M.S.,Mehzabeen, N.,Baird, N.J.,Battalie, K.P.,Ross, D.,Lovell, S.,Carlow, C.K.,Suga, H.,Inglese, J. Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases. Nat Commun, 8:14932-14932, 2017 Cited by PubMed: 28368002DOI: 10.1038/ncomms14932 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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