3LMG
Crystal structure of the ERBB3 kinase domain in complex with AMP-PNP
Summary for 3LMG
Entry DOI | 10.2210/pdb3lmg/pdb |
Descriptor | Receptor tyrosine-protein kinase erbB-3, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
Functional Keywords | erbb3, her3, tyrosine kinase domain, amp-pnp, nucleotide binding, transferase |
Biological source | Homo sapiens (human) |
Cellular location | Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: P21860 |
Total number of polymer chains | 2 |
Total formula weight | 78528.14 |
Authors | Shi, F.,Lemmon, M.A. (deposition date: 2010-01-30, release date: 2010-04-21, Last modification date: 2023-09-06) |
Primary citation | Shi, F.,Telesco, S.E.,Liu, Y.,Radhakrishnan, R.,Lemmon, M.A. ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation. Proc.Natl.Acad.Sci.USA, 107:7692-7697, 2010 Cited by PubMed: 20351256DOI: 10.1073/pnas.1002753107 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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