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5NMS

Hsp21 dodecamer, structural model based on cryo-EM and homology modelling

Replaces:  5MB8
Summary for 5NMS
Entry DOI10.2210/pdb5nms/pdb
EMDB information3459
Descriptor25.3 kDa heat shock protein, chloroplastic (2 entities in total)
Functional Keywordsstress response, heat shock protein, chaperone, all-beta greek key
Biological sourceArabidopsis thaliana (Mouse-ear cress)
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Cellular locationPlastid, chloroplast : P31170 P31170
Total number of polymer chains12
Total formula weight169027.29
Authors
Rutsdottir, G.,Harmark, J.,Koeck, P.J.B.,Hebert, H.,Soderberg, C.A.G.,Emanuelsson, C. (deposition date: 2017-04-07, release date: 2017-05-03, Last modification date: 2017-09-13)
Primary citationRutsdottir, G.,Harmark, J.,Weide, Y.,Hebert, H.,Rasmussen, M.I.,Wernersson, S.,Respondek, M.,Akke, M.,Hjrup, P.,Koeck, P.J.B.,Soderberg, C.A.G.,Emanuelsson, C.
Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity.
J. Biol. Chem., 292:8103-8121, 2017
Cited by
PubMed: 28325834
DOI: 10.1074/jbc.M116.766816
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (10 Å)
Structure validation

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