3beg Summary

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Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2

The structure was published by Ngo, J.C., Giang, K., Chakrabarti, S., et al., Fu, X.-D., Adams, J.A., and Ghosh, G., in 2008 in a paper entitled "A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.9 Å and deposited in 2007.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Serine/threonine-protein kinase SRPK1 and Splicing factor, arginine/serine-rich 1.

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 heterodimers.

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 SRPK1 Q96SB4 (58-255) (SRPK1_HUMAN)search ,
Q96SB4 (474-655) (SRPK1_HUMAN)search
Homo sapienssearch ,
Homo sapienssearch
< 90% ,
< 90%
381 91%
B Splicing factor, arginine/serine-rich 1 Q07955 (105-219) (SRSF1_HUMAN)search Homo sapienssearch < 90% 115 74%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
Q96SB4 (58 - 255) Serine/threonine-protein kinase SRPK1 Homo sapiens
Q07955 (105 - 219) Splicing factor, arginine/serine-rich 1 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search Protein kinase domainsearch
B Canonical RBDsearch RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)search

Chain ID Biological process (GO) Molecular function (GO)
A (Q96SB4) protein phosphorylationsearch protein kinase activitysearch protein serine/threonine kinase activitysearch ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch
B (Q07955) regulation of mRNA stabilitysearch regulation of transcription, DNA-templatedsearch regulation of translationsearch regulation of mRNA splicing, via spliceosomesearch mRNA bindingsearch nucleic acid bindingsearch nucleotide bindingsearch

Chain InterPro annotation
A Protein kinase domainsearch Serine/threonine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch
B RNA recognition motif domainsearch Nucleotide-binding alpha-beta plait domainsearch Serine/arginine-rich splicing factor 1search