Structure of the extracellular domain of human epidermal growth factor (EGF) receptor in an inactive (low pH) complex with EGF.

Summary for 1NQL

Descriptorepidermal growth factor receptor, epidermal growth factor, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordscell surface receptor, tyrosine kinase, glycoprotein, endosomal, growth factor, auto-inhibition, hormone-growth factor receptor complex, hormone/growth factor receptor
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total molecular weight78146.34
Ferguson, K.M.,Lemmon, M.A. (deposition date: 2003-01-21, release date: 2003-03-11, Last modification date: 2020-07-29)
Primary citation
Ferguson, K.M.,Berger, M.B.,Mendrola, J.M.,Cho, H.,Leahy, D.J.,Lemmon, M.A.
EGF activates its receptor by removing interactions that auto-inhibit ectodomain dimerization
Mol.Cell, 11:507-517, 2003
PubMed: 12620237 (PDB entries with the same primary citation)
DOI: 10.1016/S1097-2765(03)00047-9
MImport into Mendeley
Experimental method

Structure validation

ClashscoreRamachandran outliersSidechain outliers17 3.5% 16.8%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-12-02