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5KGN

1.95A resolution structure of independent phosphoglycerate mutase from C. elegans in complex with a macrocyclic peptide inhibitor (2d)

Summary for 5KGN
Entry DOI10.2210/pdb5kgn/pdb
Related5KGL 5KGM
Descriptor2,3-bisphosphoglycerate-independent phosphoglycerate mutase, macrocyclic peptide inhibitor, CHLORIDE ION, ... (8 entities in total)
Functional Keywordsmetal binding, coupled enzyme assay, hts, structure activity relationship, rapid systems, high throughput enzymology, isomerase
Biological sourceCaenorhabditis elegans
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Total number of polymer chains4
Total formula weight120870.56
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 citationYu, 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: 28368002
DOI: 10.1038/ncomms14932
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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