2w5b Summary

pdbe.org/2w5b
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Human Nek2 kinase ATPgammaS-bound

The structure was published by Westwood, I., Cheary, D.M., Baxter, J.E., et al., Van Montfort, R.L., Fry, A.M., and Bayliss, R., in 2009 in a paper entitled "Insights Into the Conformational Variability and Regulation of Human Nek2 Kinase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2008.

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

The PDB entry contains the structure of SERINE/THREONINE-PROTEIN KINASE NEK2. This molecule has the UniProt identifier P51955 (NEK2_HUMAN)search. The sample contained 279 residues which is < 90% of the natural sequence. Out of 279 residues 266 were observed and are deposited in the PDB.

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 is most likely monomeric.

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 SERINE/THREONINE-PROTEIN KINASE NEK2 P51955 (1-271) (NEK2_HUMAN)search Homo sapienssearch < 90% 279 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P51955 (1 - 271) SERINE/THREONINE-PROTEIN KINASE NEK2 Homo sapiens

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

Chain ID Molecular function (GO) Biological process (GO)
A (P51955) ATP bindingsearch protein serine/threonine kinase activitysearch protein kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch protein phosphorylationsearch

Chain InterPro annotation
A Protein kinase domainsearch Serine/threonine/dual specificity protein kinase, catalytic domainsearch Serine/threonine-protein kinase, active sitesearch Protein kinase-like domainsearch