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5KGL

2.45A resolution structure of Apo independent phosphoglycerate mutase from C. elegans (orthorhombic form)

Summary for 5KGL
Entry DOI10.2210/pdb5kgl/pdb
Related5KGM 5KGN
Descriptor2,3-bisphosphoglycerate-independent phosphoglycerate mutase, CHLORIDE ION, MANGANESE (II) ION, ... (6 entities in total)
Functional Keywordsmetal binding, coupled enzyme assay, hts, structure activity relationship, rapid systems, high throughput enzymology, isomerase
Biological sourceCaenorhabditis elegans
Total number of polymer chains2
Total formula weight122630.04
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 (2.45 Å)
Structure validation

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