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3GGF

Crystal structure of human Serine/threonine-protein kinase MST4 in complex with an quinazolin

Summary for 3GGF
Entry DOI10.2210/pdb3ggf/pdb
DescriptorSerine/threonine-protein kinase MST4, CADMIUM ION, [4-({4-[(5-CYCLOPROPYL-1H-PYRAZOL-3-YL)AMINO]QUINAZOLIN-2-YL}IMINO)CYCLOHEXA-2,5-DIEN-1-YL]ACETONITRILE, ... (4 entities in total)
Functional Keywordsserine/threonine-protein kinase, structural genomics, structural genomics consortium, sgc, apoptosis, atp-binding, golgi apparatus, kinase, magnesium, metal-binding, nucleotide-binding, phosphoprotein, transferase
Biological sourceHomo sapiens (Human)
Cellular locationCytoplasm : Q9P289
Total number of polymer chains2
Total formula weight69271.27
Authors
Primary citationRecord, C.J.,Chaikuad, A.,Rellos, P.,Das, S.,Pike, A.C.,Fedorov, O.,Marsden, B.D.,Knapp, S.,Lee, W.H.
Structural comparison of human mammalian ste20-like kinases
Plos One, 5:e11905-e11905, 2010
Cited by
PubMed Abstract: The serine/threonine mammalian Ste-20 like kinases (MSTs) are key regulators of apoptosis, cellular proliferation as well as polarization. Deregulation of MSTs has been associated with disease progression in prostate and colorectal cancer. The four human MSTs are regulated differently by C-terminal regions flanking the catalytic domains.
PubMed: 20730082
DOI: 10.1371/journal.pone.0011905
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.35 Å)
Structure validation

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