4LGD: Serine/threonine-protein kinase 3
Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5. Determined by X-ray diffraction at 3.05 Å resolution. Released 18 Sept 2013.
- Method
- X-ray diffraction
- Resolution
- 3.05 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 12,785
- Mol. weight
- 201.41 kDa
- Ligands
- ANP, MG
- Released
- 18 Sept 2013
Explore 4LGD in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4LGD contains 96 α-helices and 38 β-strands across 8 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: 23 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-20 | 4 | |
| α-helix | 23-25 | 3 | |
| β-strand | 27-35 | 9 | 1 |
| β-strand | 40-46 | 7 | 1 |
| β-strand | 52-59 | 8 | 1 |
| α-helix | 64-75 | 12 | |
| 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 | 177-180 | 4 | |
| α-helix | 190-195 | 6 | |
| α-helix | 200-216 | 17 | |
| α-helix | 226-232 | 7 | |
| α-helix | 237-239 | 3 | |
| α-helix | 244-246 | 3 | |
| α-helix | 249-258 | 10 | |
| α-helix | 267-268 | 2 | |
| α-helix | 269-272 | 4 | |
| α-helix | 276-279 | 4 | |
| α-helix | 281-283 | 3 | |
| α-helix | 285-309 | 25 | |
| α-helix | 445-453 | 9 | |
| α-helix | 457-460 | 4 | |
| α-helix | 464-473 | 10 | |
| α-helix | 475-487 | 13 | |
Chain B: 21 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-26 | 4 | |
| β-strand | 27-35 | 9 | 3 |
| β-strand | 40-46 | 7 | 3 |
| β-strand | 51-59 | 9 | 3 |
| α-helix | 64-75 | 12 | |
| β-strand | 79 | 1 | 4 |
| 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 | 117-119 | 3 | |
| α-helix | 120-139 | 20 | |
| α-helix | 149-151 | 3 | |
| β-strand | 152-154 | 3 | 4 |
| β-strand | 160-162 | 3 | 4 |
| 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 | 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 | 288-311 | 24 | |
| α-helix | 445-447 | 3 | |
| α-helix | 456-458 | 3 | |
| α-helix | 464-487 | 24 | |
Chain C: 22 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-15 | 3 | |
| α-helix | 23-25 | 3 | |
| β-strand | 27-29 | 3 | 5 |
| β-strand | 41-46 | 6 | 5 |
| β-strand | 52-59 | 8 | 5 |
| α-helix | 64-75 | 12 | |
| β-strand | 79 | 1 | 6 |
| β-strand | 82 | 1 | 6 |
| 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 | 177-180 | 4 | |
| α-helix | 190-195 | 6 | |
| α-helix | 202-216 | 15 | |
| α-helix | 226-235 | 10 | |
| 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 | 285-311 | 27 | |
| α-helix | 445-447 | 3 | |
| α-helix | 456-473 | 18 | |
| α-helix | 475-489 | 15 | |
Chain D: 22 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14-15 | 2 | |
| α-helix | 16-20 | 5 | |
| α-helix | 23-26 | 4 | |
| β-strand | 27-35 | 9 | 7 |
| β-strand | 40-46 | 7 | 7 |
| β-strand | 51-59 | 9 | 7 |
| α-helix | 64-75 | 12 | |
| β-strand | 82 | 1 | 8 |
| β-strand | 85-91 | 7 | 7 |
| β-strand | 94-100 | 7 | 7 |
| β-strand | 105-106 | 2 | 8 |
| α-helix | 107-113 | 7 | |
| α-helix | 120-139 | 20 | |
| α-helix | 149-151 | 3 | |
| β-strand | 152-154 | 3 | 8 |
| β-strand | 160-162 | 3 | 8 |
| α-helix | 176-180 | 5 | |
| 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 | 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 | 288-310 | 23 | |
| α-helix | 460-473 | 14 | |
| α-helix | 475-488 | 14 | |
Chains E and G: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 369-371 | 3 | |
| α-helix | 374-410 | 37 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 374-397 | 24 | |
Chain H: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 369-371 | 3 | |
| α-helix | 374-392 | 19 | |
| α-helix | 396-403 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Serine/threonine-protein kinase 3 | A, B, C, D | protein | 378 | Homo sapiens | Q13188 (AlphaFold model) |
| Ras association domain family member 5, RASSF5 | E, F, G, H | protein | 49 | Homo sapiens | Q8WWW0 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>4LGD_1 Serine/threonine-protein kinase 3 (chains A, B, C, D)
MHHHHHHGSSKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVP
VESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLI
EDEIATILKSTLKGLEYLHFMRKIHRNIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRN
TVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPP
TFRKPELWSDDFTDFVKKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEAMEIKA
KRHEEQQRELEEEENWKVPQDGDFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAK
RQPILDAMDAKKRRQQNF
Sequence of entity 2 (E, F, G, H), FASTA
>4LGD_2 Ras association domain family member 5, RASSF5 (chains E, F, G, H)
GEVEWDAFSIPELQNFLTILEKEEQDKIQQVQKKYDKFRQKLEEALRES
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 4 |
| MG | Magnesium ion | Mg | 4 |
Water and common crystallization additives (SO4, NA) are not listed.
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
- 4LG4 2.42 Å, Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5
- 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
Browse structure collections
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