1rqq Summary

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Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of APS

The structure was published by Hu, J., Liu, J., Ghirlando, R., Saltiel, A.R., and Hubbard, S.R., in 2003 in a paper entitled "Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2003.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 3 biomacromolecules, namely Insulin receptor, adaptor protein APS, and BISUBSTRATE INHIBITOR.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms heterohexamers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Insulin receptor P06213 (1005-1310) (INSR_HUMAN)search Homo sapienssearch < 90% 306 97%
B Insulin receptor P06213 (1005-1310) (INSR_HUMAN)search Homo sapienssearch < 90% 306 97%
C adaptor protein APS Q9Z200 (401-510) (SH2B2_RAT)search Rattus norvegicussearch < 90% 114 72%
D adaptor protein APS Q9Z200 (401-510) (SH2B2_RAT)search Rattus norvegicussearch < 90% 114 72%
E BISUBSTRATE INHIBITOR Not available
Not available Not available 18 77%
F BISUBSTRATE INHIBITOR Not available
Not available Not available 18 77%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P06213 (1005 - 1310) Insulin receptor Homo sapiens
Q9Z200 (401 - 510) adaptor protein APS Rattus norvegicus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Protein kinases, catalytic subunitsearch Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search Protein tyrosine kinasesearch
C, D SH2 domainsearch SHC Adaptor Proteinsearch SH2 domainsearch
E, F

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P06213) protein kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch ATP bindingsearch protein tyrosine kinase activitysearch transmembrane receptor protein tyrosine kinase activitysearch protein phosphorylationsearch transmembrane receptor protein tyrosine kinase signaling pathwaysearch membranesearch

Chain InterPro annotation
A, B Protein kinase domainsearch Serine-threonine/tyrosine-protein kinase catalytic domainsearch Tyrosine-protein kinase, receptor class II, conserved sitesearch Tyrosine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch Tyrosine-protein kinase, catalytic domainsearch
C, D SH2 domainsearch
E, F