Crystal structure of human co-chaperone protein HscB

Summary for 3BVO

DescriptorCo-chaperone protein HscB, mitochondrial precursor, ZINC ION, SULFATE ION (3 entities in total)
Functional Keywordsco-chaperone protein hscb, structural genomics medical relevance, protein structure initiative, psi-2, center for eukaryotic structural genomics, cesg, mitochondrion, transit peptide, chaperone
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm  Q8IWL3
Total number of polymer chains2
Total molecular weight49022.5
Bitto, E.,Bingman, C.A.,McCoy, J.G.,Wesenberg, G.E.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2008-01-07, release date: 2008-01-15, Last modification date: 2017-10-25)
Primary citation
Bitto, E.,Bingman, C.A.,Bittova, L.,Kondrashov, D.A.,Bannen, R.M.,Fox, B.G.,Markley, J.L.,Phillips, G.N.
Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain.
J.Biol.Chem., 283:30184-30192, 2008
PubMed: 18713742 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.M804746200
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.28170.5%4.4%3.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution