1IRK

CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE HUMAN INSULIN RECEPTOR

Summary for 1IRK

Entry DOI	10.2210/pdb1irk/pdb
Descriptor	INSULIN RECEPTOR TYROSINE KINASE DOMAIN, ETHYL MERCURY ION (3 entities in total)
Functional Keywords	transferase (phosphotransferase)
Biological source	Homo sapiens (human)
Cellular location	Membrane; Single-pass type I membrane protein: P06213
Total number of polymer chains	1
Total formula weight	35252.11
Authors	Hubbard, S.R.,Wei, L.,Ellis, L.,Hendrickson, W.A. (deposition date: 1995-01-02, release date: 1995-02-27, Last modification date: 2024-02-07)
Primary citation	Hubbard, S.R.,Wei, L.,Ellis, L.,Hendrickson, W.A. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature, 372:746-754, 1994 Cited by PubMed Abstract: The X-ray crystal structure of the tyrosine kinase domain of the human insulin receptor has been determined by multiwavelength anomalous diffraction phasing and refined to 2.1 A resolution. The structure reveals the determinants of substrate preference for tyrosine rather than serine or threonine and a novel autoinhibition mechanism whereby one of the tyrosines that is autophosphorylated in response to insulin, Tyr 1,162, is bound in the active site. PubMed: 7997262 DOI: 10.1038/372746a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation