4LG4: Serine/threonine-protein kinase 3

Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5. Determined by X-ray diffraction at 2.42 Å resolution. Released 18 Sept 2013.

Method
X-ray diffraction
Resolution
2.42 Å
Organism
Homo sapiens
Chains
6
Atoms
13,447
Mol. weight
204.2 kDa
Released
18 Sept 2013

Explore 4LG4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4LG4 contains 123 α-helices and 53 β-strands across 6 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: 21 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix23-264
β-strand27-3481
β-strand40-4671
β-strand52-5871
α-helix64-7613
β-strand8212
β-strand85-9171
β-strand94-10071
β-strand105-10622
α-helix107-1148
α-helix117-1193
α-helix120-13920
α-helix149-1513
β-strand152-15432
β-strand160-16232
α-helix170-1723
α-helix175-1828
α-helix190-1956
α-helix201-21616
α-helix226-23510
α-helix237-2393
α-helix244-2463
α-helix249-25810
α-helix263-2653
α-helix267-2682
α-helix269-2724
α-helix276-2794
α-helix281-2833
α-helix284-2874
α-helix288-30619
Chain B: 20 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix23-264
β-strand27-3483
β-strand41-4663
β-strand52-5873
α-helix64-7613
β-strand8214
β-strand85-9173
β-strand94-10073
β-strand105-10624
α-helix107-1148
α-helix120-13920
α-helix149-1513
β-strand152-15434
β-strand160-16234
α-helix175-1839
α-helix184-1874
α-helix190-1934
α-helix202-21615
α-helix226-23510
α-helix237-2393
α-helix244-2463
α-helix249-25810
α-helix263-2653
α-helix267-2682
α-helix269-2724
α-helix276-2794
α-helix281-2833
α-helix284-2874
α-helix288-30720
Chain C: 22 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix23-264
β-strand27-3595
β-strand40-4675
β-strand52-5985
α-helix64-7512
β-strand8216
α-helix83-842
β-strand85-9175
β-strand94-10075
β-strand105-10626
α-helix107-1148
α-helix117-1193
α-helix120-13920
α-helix149-1513
β-strand152-15436
β-strand160-16236
α-helix165-1673
α-helix175-1828
α-helix190-1956
α-helix202-21615
α-helix226-23510
α-helix237-2393
α-helix244-2463
α-helix249-25810
α-helix263-2653
α-helix267-2682
α-helix269-2724
α-helix276-2794
α-helix281-2833
α-helix284-2874
α-helix288-30619
Chain D: 19 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand29-3247
β-strand42-4437
β-strand53-5647
α-helix64-7411
β-strand8218
α-helix83-842
β-strand85-8847
β-strand97-10047
β-strand10618
α-helix107-1148
α-helix117-1193
α-helix120-13920
α-helix149-1513
β-strand152-15438
β-strand160-16238
α-helix190-1945
α-helix201-21616
α-helix226-23510
α-helix237-2393
α-helix244-2463
α-helix249-25810
α-helix263-2653
α-helix267-2682
α-helix269-2724
α-helix276-2794
α-helix281-2833
α-helix284-2874
α-helix288-30619
Chain E: 21 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix23-264
β-strand27-3269
β-strand40-4679
β-strand51-5779
α-helix65-7612
β-strand82110
α-helix83-842
β-strand85-9179
β-strand94-10079
α-helix107-1148
α-helix120-13920
α-helix149-1513
β-strand152-154310
β-strand160-162310
α-helix165-1673
α-helix185-1873
α-helix190-1956
α-helix202-21615
α-helix226-23510
α-helix237-2393
α-helix244-2463
α-helix249-25810
α-helix263-2653
α-helix267-2682
α-helix269-2724
α-helix276-2794
α-helix281-2833
α-helix284-2863
α-helix288-30720
Chain F: 20 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix23-264
β-strand27-34811
β-strand41-46611
β-strand52-56511
α-helix64-7512
β-strand82112
α-helix83-842
β-strand85-91711
β-strand94-100711
β-strand106112
α-helix107-1148
α-helix120-13920
α-helix149-1513
β-strand152-154312
β-strand160-162312
α-helix190-1945
α-helix202-21615
α-helix226-23510
α-helix237-2393
α-helix244-2463
α-helix249-25810
α-helix263-2653
α-helix267-2682
α-helix269-2724
α-helix276-2794
α-helix281-2833
α-helix284-2874
α-helix288-30215
α-helix306-3094

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein kinase 3A, B, C, D, E, Fprotein299Homo sapiensQ13188 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>4LG4_1 Serine/threonine-protein kinase 3 (chains A, B, C, D, E, F)
GEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIM
QQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLIEDEIATILKSTLKGL
EYLHFMRKIHRNIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQ
EIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDF
VKKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEAMEIKAKRHEEQQRELEEEE

Primary citation

Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5. Ni, L., Li, S., Yu, J. et al. Structure (2013) 21:1757-1768. DOI 10.1016/j.str.2013.07.008 · PubMed

Other PDB entries of the same protein (UniProt Q13188 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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