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
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-26 | 4 | |
| β-strand | 27-34 | 8 | 1 |
| β-strand | 40-46 | 7 | 1 |
| β-strand | 52-58 | 7 | 1 |
| α-helix | 64-76 | 13 | |
| β-strand | 82 | 1 | 2 |
| β-strand | 85-91 | 7 | 1 |
| β-strand | 94-100 | 7 | 1 |
| β-strand | 105-106 | 2 | 2 |
| α-helix | 107-114 | 8 | |
| α-helix | 117-119 | 3 | |
| α-helix | 120-139 | 20 | |
| α-helix | 149-151 | 3 | |
| β-strand | 152-154 | 3 | 2 |
| β-strand | 160-162 | 3 | 2 |
| α-helix | 170-172 | 3 | |
| α-helix | 175-182 | 8 | |
| α-helix | 190-195 | 6 | |
| α-helix | 201-216 | 16 | |
| α-helix | 226-235 | 10 | |
| α-helix | 237-239 | 3 | |
| α-helix | 244-246 | 3 | |
| α-helix | 249-258 | 10 | |
| α-helix | 263-265 | 3 | |
| α-helix | 267-268 | 2 | |
| α-helix | 269-272 | 4 | |
| α-helix | 276-279 | 4 | |
| α-helix | 281-283 | 3 | |
| α-helix | 284-287 | 4 | |
| α-helix | 288-306 | 19 | |
Chain B: 20 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-26 | 4 | |
| β-strand | 27-34 | 8 | 3 |
| β-strand | 41-46 | 6 | 3 |
| β-strand | 52-58 | 7 | 3 |
| α-helix | 64-76 | 13 | |
| β-strand | 82 | 1 | 4 |
| β-strand | 85-91 | 7 | 3 |
| β-strand | 94-100 | 7 | 3 |
| β-strand | 105-106 | 2 | 4 |
| α-helix | 107-114 | 8 | |
| α-helix | 120-139 | 20 | |
| α-helix | 149-151 | 3 | |
| β-strand | 152-154 | 3 | 4 |
| β-strand | 160-162 | 3 | 4 |
| α-helix | 175-183 | 9 | |
| α-helix | 184-187 | 4 | |
| α-helix | 190-193 | 4 | |
| α-helix | 202-216 | 15 | |
| α-helix | 226-235 | 10 | |
| α-helix | 237-239 | 3 | |
| α-helix | 244-246 | 3 | |
| α-helix | 249-258 | 10 | |
| α-helix | 263-265 | 3 | |
| α-helix | 267-268 | 2 | |
| α-helix | 269-272 | 4 | |
| α-helix | 276-279 | 4 | |
| α-helix | 281-283 | 3 | |
| α-helix | 284-287 | 4 | |
| α-helix | 288-307 | 20 | |
Chain C: 22 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-26 | 4 | |
| β-strand | 27-35 | 9 | 5 |
| β-strand | 40-46 | 7 | 5 |
| β-strand | 52-59 | 8 | 5 |
| α-helix | 64-75 | 12 | |
| β-strand | 82 | 1 | 6 |
| α-helix | 83-84 | 2 | |
| β-strand | 85-91 | 7 | 5 |
| β-strand | 94-100 | 7 | 5 |
| β-strand | 105-106 | 2 | 6 |
| α-helix | 107-114 | 8 | |
| α-helix | 117-119 | 3 | |
| α-helix | 120-139 | 20 | |
| α-helix | 149-151 | 3 | |
| β-strand | 152-154 | 3 | 6 |
| β-strand | 160-162 | 3 | 6 |
| α-helix | 165-167 | 3 | |
| α-helix | 175-182 | 8 | |
| α-helix | 190-195 | 6 | |
| α-helix | 202-216 | 15 | |
| α-helix | 226-235 | 10 | |
| α-helix | 237-239 | 3 | |
| α-helix | 244-246 | 3 | |
| α-helix | 249-258 | 10 | |
| α-helix | 263-265 | 3 | |
| α-helix | 267-268 | 2 | |
| α-helix | 269-272 | 4 | |
| α-helix | 276-279 | 4 | |
| α-helix | 281-283 | 3 | |
| α-helix | 284-287 | 4 | |
| α-helix | 288-306 | 19 | |
Chain D: 19 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 29-32 | 4 | 7 |
| β-strand | 42-44 | 3 | 7 |
| β-strand | 53-56 | 4 | 7 |
| α-helix | 64-74 | 11 | |
| β-strand | 82 | 1 | 8 |
| α-helix | 83-84 | 2 | |
| β-strand | 85-88 | 4 | 7 |
| β-strand | 97-100 | 4 | 7 |
| β-strand | 106 | 1 | 8 |
| α-helix | 107-114 | 8 | |
| α-helix | 117-119 | 3 | |
| α-helix | 120-139 | 20 | |
| α-helix | 149-151 | 3 | |
| β-strand | 152-154 | 3 | 8 |
| β-strand | 160-162 | 3 | 8 |
| α-helix | 190-194 | 5 | |
| α-helix | 201-216 | 16 | |
| α-helix | 226-235 | 10 | |
| α-helix | 237-239 | 3 | |
| α-helix | 244-246 | 3 | |
| α-helix | 249-258 | 10 | |
| α-helix | 263-265 | 3 | |
| α-helix | 267-268 | 2 | |
| α-helix | 269-272 | 4 | |
| α-helix | 276-279 | 4 | |
| α-helix | 281-283 | 3 | |
| α-helix | 284-287 | 4 | |
| α-helix | 288-306 | 19 | |
Chain E: 21 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-26 | 4 | |
| β-strand | 27-32 | 6 | 9 |
| β-strand | 40-46 | 7 | 9 |
| β-strand | 51-57 | 7 | 9 |
| α-helix | 65-76 | 12 | |
| β-strand | 82 | 1 | 10 |
| α-helix | 83-84 | 2 | |
| β-strand | 85-91 | 7 | 9 |
| β-strand | 94-100 | 7 | 9 |
| α-helix | 107-114 | 8 | |
| α-helix | 120-139 | 20 | |
| α-helix | 149-151 | 3 | |
| β-strand | 152-154 | 3 | 10 |
| β-strand | 160-162 | 3 | 10 |
| α-helix | 165-167 | 3 | |
| α-helix | 185-187 | 3 | |
| α-helix | 190-195 | 6 | |
| α-helix | 202-216 | 15 | |
| α-helix | 226-235 | 10 | |
| α-helix | 237-239 | 3 | |
| α-helix | 244-246 | 3 | |
| α-helix | 249-258 | 10 | |
| α-helix | 263-265 | 3 | |
| α-helix | 267-268 | 2 | |
| α-helix | 269-272 | 4 | |
| α-helix | 276-279 | 4 | |
| α-helix | 281-283 | 3 | |
| α-helix | 284-286 | 3 | |
| α-helix | 288-307 | 20 | |
Chain F: 20 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-26 | 4 | |
| β-strand | 27-34 | 8 | 11 |
| β-strand | 41-46 | 6 | 11 |
| β-strand | 52-56 | 5 | 11 |
| α-helix | 64-75 | 12 | |
| β-strand | 82 | 1 | 12 |
| α-helix | 83-84 | 2 | |
| β-strand | 85-91 | 7 | 11 |
| β-strand | 94-100 | 7 | 11 |
| β-strand | 106 | 1 | 12 |
| α-helix | 107-114 | 8 | |
| α-helix | 120-139 | 20 | |
| α-helix | 149-151 | 3 | |
| β-strand | 152-154 | 3 | 12 |
| β-strand | 160-162 | 3 | 12 |
| α-helix | 190-194 | 5 | |
| α-helix | 202-216 | 15 | |
| α-helix | 226-235 | 10 | |
| α-helix | 237-239 | 3 | |
| α-helix | 244-246 | 3 | |
| α-helix | 249-258 | 10 | |
| α-helix | 263-265 | 3 | |
| α-helix | 267-268 | 2 | |
| α-helix | 269-272 | 4 | |
| α-helix | 276-279 | 4 | |
| α-helix | 281-283 | 3 | |
| α-helix | 284-287 | 4 | |
| α-helix | 288-302 | 15 | |
| α-helix | 306-309 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Serine/threonine-protein kinase 3 | A, B, C, D, E, F | protein | 299 | Homo sapiens | Q13188 (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:
- 4L0N 1.4 Å, Crystal structure of STK3 (MST2) SARAH domain
- 4HKD 1.5 Å, Crystal structure of human MST2 SARAH domain
- 6AR2 1.55 Å, Structure of human SLMAP FHA domain in complex with pMST2
- 4OH9 1.7 Å, Crystal Structure of the human MST2 SARAH homodimer
- 8A66 1.9 Å, Crystal structure of MST2 in complex with XMU-MP-1
- 3WWS 2.01 Å, Crystal structure of Serine/threonine-protein kinase 3
- 5DH3 2.47 Å, Crystal structure of MST2 in complex with XMU-MP-1
- 5BRM 2.65 Å, Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in…
- 6AO5 2.96 Å, Crystal structure of human MST2 in complex with SAV1 SARAH domain
- 4LGD 3.05 Å, Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5
Browse structure collections
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