5OQ0

Crystal structure of transthyretin mutant 87-110-117

Summary for 5OQ0

DescriptorTransthyretin (2 entities in total)
Functional Keywordsamyloidosis, homo-tetramer, retinol-binding protein, ttr, transport protein
Biological sourceHomo sapiens (Human)
Cellular locationSecreted P02766
Total number of polymer chains1
Total molecular weight13821.46
Authors
Zanotti, G.,Vallese, F.,Berni, R. (deposition date: 2017-08-10, release date: 2017-12-27)
Primary citation
Zanotti, G.,Vallese, F.,Ferrari, A.,Menozzi, I.,Saldano, T.E.,Berto, P.,Fernandez-Alberti, S.,Berni, R.
Structural and dynamics evidence for scaffold asymmetric flexibility of the human transthyretin tetramer.
PLoS ONE, 12:e0187716-e0187716, 2017
PubMed: 29240759 (PDB entries with the same primary citation)
DOI: 10.1371/journal.pone.0187716
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.94 Å)
?

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.2681002.1%2.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 5oq0
no rotation
Molmil generated image of 5oq0
rotated about x axis by 90°
Molmil generated image of 5oq0
rotated about y axis by 90°

More Biological unit images

Molmil generated image of 5oq0
no rotation
Molmil generated image of 5oq0
rotated about x axis by 90°
Molmil generated image of 5oq0
rotated about y axis by 90°
(*)In the case of coarse surface representation, the asymmetric unit is shown as red ribbon representation.
Coordinate files for Biological unit (5oq0.pdb1.gz [153.6 KB])