3BEG: Serine/threonine-protein kinase SRPK1

Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2. Determined by X-ray diffraction at 2.9 Å resolution. Released 1 Apr 2008.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Homo sapiens
Chains
2
Atoms
3,446
Mol. weight
57.18 kDa
Ligands
SEP, ALA, ANP
Released
1 Apr 2008

Explore 3BEG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BEG contains 23 α-helices and 22 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 20 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand75-7621
β-strand80-8891
β-strand92-9981
β-strand105-11171
α-helix115-13218
β-strand14412
α-helix145-1462
β-strand147-15151
β-strand15413
β-strand15913
β-strand162-16541
β-strand17112
α-helix172-1787
α-helix186-20116
α-helix202-2065
β-strand209-21024
α-helix216-2183
β-strand219-22132
α-helix225-2328
α-helix485-4873
β-strand493-49532
β-strand502-50324
α-helix515-5173
α-helix520-5245
α-helix531-54616
α-helix561-57313
α-helix576-5772
α-helix578-5814
α-helix587-5904
β-strand59115
β-strand59715
α-helix608-6147
α-helix622-6254
α-helix627-6337
α-helix644-6485
α-helix651-6544
Chain B: 3 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand123-12756
α-helix136-1416
α-helix142-1443
β-strand147-15266
β-strand157-16266
α-helix165-17511
β-strand17917
β-strand18917
β-strand191-19446

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein kinase SRPK1Aprotein381Homo sapiensQ96SB4 (AlphaFold model)
Splicing factor, arginine/serine-rich 1Bprotein115Homo sapiensQ07955 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3BEG_1 Serine/threonine-protein kinase SRPK1 (chains A)
DPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHY
TETALDEIRLLKSVRNSDPNDPNREMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWII
KSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATE
WQRSGAPPPSGSAVSTAPATAGNFLVNPLEPKNAEKLKVKIADLGNACWVHKHFTEDIQT
RQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEEYTRDEDHIALIIELLG
KVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLFEVLVEKYEWSQEEAAGFTDFLLPML
ELIPEKRATAAECLRHPWLNS
Sequence of entity 2 (B), FASTA
>3BEG_2 Splicing factor, arginine/serine-rich 1 (chains B)
GGAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVR
KEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRS

Ligands and cofactors

IDNameFormulaCopies
SEPPhosphoserineC3 H8 N O6 P1
ALAAlanineC3 H7 N O21
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P31

Primary citation

A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1. Ngo, J.C., Giang, K., Chakrabarti, S. et al. Mol Cell (2008) 29:563-576. DOI 10.1016/j.molcel.2007.12.017 · PubMed

Other PDB entries of the same protein (UniProt Q96SB4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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