2g2h Summary


A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain

The structure was published by Levinson, N.M., Kuchment, O., Shen, K., et al., Karplus, M., Cole, P.A., and Kuriyan, J., in 2006 in a paper entitled "A SRC-like inactive conformation in the abl tyrosine kinase domain." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2006.

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

This PDB entry contains multiple copies of the structure of Abl Tyrosine.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 Abl Tyrosine P00519 (229-512) (ABL1_HUMAN)search Homo sapienssearch < 90% 287 94%
B Abl Tyrosine P00519 (229-512) (ABL1_HUMAN)search Homo sapienssearch < 90% 287 94%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00519 (229 - 512) Abl Tyrosine Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A, B Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search Protein tyrosine kinasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P00519) transferase activity, transferring phosphorus-containing groupssearch ATP bindingsearch protein kinase activitysearch protein tyrosine kinase activitysearch protein phosphorylationsearch

Chain InterPro annotation
A, B 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