2gs6 Summary

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Crystal Structure of the active EGFR kinase domain in complex with an ATP analog-peptide conjugate

The structure was published by Zhang, X., Gureasko, J., Shen, K., Cole, P.A., and Kuriyan, J., in 2006 in a paper entitled "An Allosteric Mechanism for Activation of the Kinase Domain of Epidermal Growth Factor Receptor" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2006.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Epidermal growth factor receptor and Peptide.

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 heterotetramers.

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 Epidermal growth factor receptor P00533 (696-1022) (EGFR_HUMAN)search Homo sapienssearch < 90% 330 94%
B Peptide Not available
Not available Not available 13 38%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00533 (696 - 1022) Epidermal growth factor receptor Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Protein kinases, catalytic subunitsearch Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search Protein tyrosine kinasesearch
B
Chain InterPro annotation
A Protein kinase domainsearch Serine-threonine/tyrosine-protein kinase catalytic domainsearch Tyrosine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch Tyrosine-protein kinase, catalytic domainsearch
B