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4PED

Mitochondrial ADCK3 employs an atypical protein kinase-like fold to enable coenzyme Q biosynthes

Summary for 4PED
Entry DOI10.2210/pdb4ped/pdb
DescriptorChaperone activity of bc1 complex-like, mitochondrial, SULFATE ION (3 entities in total)
Functional Keywordsprotein kinase-like, coenzyme q biosynthesis, mitochondrial, membrane associated, structural genomics, psi-biology, mitochondrial protein partnership, mpp, transferase
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight46143.50
Authors
Primary citationStefely, J.A.,Reidenbach, A.G.,Ulbrich, A.,Oruganty, K.,Floyd, B.J.,Jochem, A.,Saunders, J.M.,Johnson, I.E.,Minogue, C.E.,Wrobel, R.L.,Barber, G.E.,Lee, D.,Li, S.,Kannan, N.,Coon, J.J.,Bingman, C.A.,Pagliarini, D.J.
Mitochondrial ADCK3 Employs an Atypical Protein Kinase-like Fold to Enable Coenzyme Q Biosynthesis.
Mol.Cell, 57:83-94, 2015
Cited by
PubMed: 25498144
DOI: 10.1016/j.molcel.2014.11.002
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.64 Å)
Structure validation

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