8XFY: RSK2 from Biortus
The Crystal Structure of RSK2 from Biortus. Determined by X-ray diffraction at 3.2 Å resolution. Released 6 Mar 2024.
- Method
- X-ray diffraction
- Resolution
- 3.2 Å
- Organism
- Homo sapiens
- Chains
- 10
- Atoms
- 22,210
- Mol. weight
- 373.05 kDa
- Ligands
- A1LU8
- Released
- 6 Mar 2024
Explore 8XFY in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8XFY contains 140 α-helices and 120 β-strands across 10 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: 15 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 62 | 1 | 1 |
| α-helix | 65-67 | 3 | |
| β-strand | 68-76 | 9 | 1 |
| β-strand | 80-87 | 8 | 1 |
| β-strand | 96-103 | 8 | 1 |
| β-strand | 114 | 1 | 2 |
| β-strand | 130 | 1 | 3 |
| β-strand | 135-138 | 4 | 1 |
| β-strand | 142-147 | 6 | 1 |
| β-strand | 153-154 | 2 | 3 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-185 | 19 | |
| β-strand | 189-191 | 3 | 4 |
| β-strand | 199-201 | 3 | 3 |
| β-strand | 207-209 | 3 | 3 |
| β-strand | 214-216 | 3 | 4 |
| α-helix | 237-240 | 4 | |
| α-helix | 248-263 | 16 | |
| α-helix | 273-282 | 10 | |
| α-helix | 283-288 | 6 | |
| α-helix | 293-302 | 10 | |
| α-helix | 307-309 | 3 | |
| α-helix | 318-322 | 5 | |
| α-helix | 325-327 | 3 | |
| α-helix | 332-336 | 5 | |
| α-helix | 341-342 | 2 | |
| α-helix | 345-347 | 3 | |
| α-helix | 351-354 | 4 | |
Chain B: 16 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 61-62 | 2 | 5 |
| α-helix | 65-67 | 3 | |
| β-strand | 68-76 | 9 | 5 |
| β-strand | 80-87 | 8 | 5 |
| β-strand | 96-102 | 7 | 5 |
| α-helix | 119-124 | 6 | |
| β-strand | 127 | 1 | 6 |
| β-strand | 130 | 1 | 6 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-138 | 6 | 5 |
| β-strand | 143-148 | 6 | 5 |
| β-strand | 153-154 | 2 | 6 |
| α-helix | 156-162 | 7 | |
| α-helix | 167-186 | 20 | |
| β-strand | 189 | 1 | 7 |
| α-helix | 196-198 | 3 | |
| β-strand | 199-201 | 3 | 6 |
| β-strand | 207-209 | 3 | 6 |
| β-strand | 216 | 1 | 7 |
| α-helix | 232-234 | 3 | |
| α-helix | 237-240 | 4 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-281 | 9 | |
| α-helix | 286-288 | 3 | |
| α-helix | 293-302 | 10 | |
| α-helix | 318-322 | 5 | |
| α-helix | 325-327 | 3 | |
| α-helix | 332-336 | 5 | |
| α-helix | 341-342 | 2 | |
Chain C: 15 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-67 | 3 | |
| β-strand | 68-76 | 9 | 8 |
| β-strand | 80-87 | 8 | 8 |
| β-strand | 96-102 | 7 | 8 |
| β-strand | 130 | 1 | 9 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-139 | 7 | 8 |
| β-strand | 142-147 | 6 | 8 |
| β-strand | 153-154 | 2 | 9 |
| α-helix | 156-162 | 7 | |
| α-helix | 167-186 | 20 | |
| β-strand | 189-190 | 2 | 10 |
| β-strand | 199-201 | 3 | 9 |
| β-strand | 207-209 | 3 | 9 |
| β-strand | 215-216 | 2 | 10 |
| α-helix | 232-234 | 3 | |
| α-helix | 237-240 | 4 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-281 | 9 | |
| α-helix | 286-288 | 3 | |
| α-helix | 293-302 | 10 | |
| α-helix | 319-322 | 4 | |
| α-helix | 325-328 | 4 | |
| α-helix | 332-336 | 5 | |
| α-helix | 341-342 | 2 | |
| α-helix | 351-354 | 4 | |
| β-strand | 357 | 1 | 2 |
Chain D: 12 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 68-76 | 9 | 11 |
| β-strand | 80-87 | 8 | 11 |
| β-strand | 96-102 | 7 | 11 |
| β-strand | 127 | 1 | 12 |
| β-strand | 130 | 1 | 12 |
| β-strand | 133-138 | 6 | 11 |
| β-strand | 143-148 | 6 | 11 |
| β-strand | 153-154 | 2 | 12 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-186 | 20 | |
| β-strand | 189-191 | 3 | 13 |
| α-helix | 196-198 | 3 | |
| β-strand | 199-201 | 3 | 12 |
| β-strand | 207-209 | 3 | 12 |
| β-strand | 214-216 | 3 | 13 |
| α-helix | 232-234 | 3 | |
| α-helix | 237-240 | 4 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-281 | 9 | |
| α-helix | 286-288 | 3 | |
| α-helix | 293-302 | 10 | |
| α-helix | 319-322 | 4 | |
| α-helix | 325-327 | 3 | |
| α-helix | 332-336 | 5 | |
Chain E: 14 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 69-76 | 8 | 14 |
| β-strand | 80-87 | 8 | 14 |
| β-strand | 95-102 | 8 | 14 |
| α-helix | 121-123 | 3 | |
| β-strand | 130 | 1 | 15 |
| β-strand | 133-137 | 5 | 14 |
| β-strand | 144-147 | 4 | 14 |
| β-strand | 154 | 1 | 15 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-187 | 21 | |
| β-strand | 189-191 | 3 | 16 |
| β-strand | 199-201 | 3 | 15 |
| β-strand | 207-209 | 3 | 15 |
| β-strand | 214-216 | 3 | 16 |
| α-helix | 232-234 | 3 | |
| α-helix | 237-240 | 4 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-281 | 9 | |
| α-helix | 283-285 | 3 | |
| α-helix | 293-302 | 10 | |
| α-helix | 307-309 | 3 | |
| α-helix | 318-322 | 5 | |
| α-helix | 325-329 | 5 | |
| α-helix | 332-336 | 5 | |
| α-helix | 341-342 | 2 | |
Chain F: 12 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-67 | 3 | |
| β-strand | 68-76 | 9 | 17 |
| β-strand | 80-87 | 8 | 17 |
| β-strand | 96-102 | 7 | 17 |
| β-strand | 130 | 1 | 18 |
| β-strand | 133-139 | 7 | 17 |
| β-strand | 142-147 | 6 | 17 |
| β-strand | 154 | 1 | 18 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-187 | 21 | |
| β-strand | 190-191 | 2 | 19 |
| β-strand | 199-201 | 3 | 18 |
| β-strand | 207-209 | 3 | 18 |
| β-strand | 214-215 | 2 | 19 |
| α-helix | 232-234 | 3 | |
| α-helix | 237-240 | 4 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-281 | 9 | |
| α-helix | 293-302 | 10 | |
| α-helix | 318-322 | 5 | |
| α-helix | 325-327 | 3 | |
| α-helix | 332-336 | 5 | |
| α-helix | 341-342 | 2 | |
Chain G: 16 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-67 | 3 | |
| β-strand | 68-76 | 9 | 20 |
| β-strand | 81-87 | 7 | 20 |
| α-helix | 90-92 | 3 | |
| β-strand | 96-103 | 8 | 20 |
| β-strand | 109 | 1 | 21 |
| β-strand | 114 | 1 | 21 |
| α-helix | 117-120 | 4 | |
| β-strand | 130 | 1 | 22 |
| β-strand | 133-139 | 7 | 20 |
| β-strand | 142-147 | 6 | 20 |
| β-strand | 154 | 1 | 22 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-187 | 21 | |
| β-strand | 189-191 | 3 | 23 |
| α-helix | 196-198 | 3 | |
| β-strand | 199-201 | 3 | 22 |
| β-strand | 207-209 | 3 | 22 |
| β-strand | 214-216 | 3 | 23 |
| α-helix | 232-234 | 3 | |
| α-helix | 237-240 | 4 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-281 | 9 | |
| α-helix | 283-286 | 4 | |
| α-helix | 293-302 | 10 | |
| α-helix | 319-322 | 4 | |
| α-helix | 325-329 | 5 | |
| α-helix | 332-336 | 5 | |
| α-helix | 341-342 | 2 | |
Chain H: 15 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 61-62 | 2 | 24 |
| α-helix | 65-67 | 3 | |
| β-strand | 68-76 | 9 | 24 |
| β-strand | 81-87 | 7 | 24 |
| α-helix | 90-92 | 3 | |
| β-strand | 96-103 | 8 | 24 |
| β-strand | 127 | 1 | 25 |
| β-strand | 130 | 1 | 25 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-138 | 6 | 24 |
| β-strand | 142-147 | 6 | 24 |
| β-strand | 154 | 1 | 25 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-185 | 19 | |
| β-strand | 189-191 | 3 | 26 |
| α-helix | 196-198 | 3 | |
| β-strand | 199-201 | 3 | 25 |
| β-strand | 207-209 | 3 | 25 |
| β-strand | 214-216 | 3 | 26 |
| α-helix | 237-240 | 4 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-281 | 9 | |
| α-helix | 284-288 | 5 | |
| α-helix | 293-302 | 10 | |
| α-helix | 318-323 | 6 | |
| α-helix | 325-327 | 3 | |
| α-helix | 332-336 | 5 | |
| α-helix | 341-342 | 2 | |
2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Ribosomal protein S6 kinase alpha-3 | A, B, C, D, E, F, G, H, I, J | protein | 320 | Homo sapiens | P51812 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J), FASTA
>8XFY_1 Ribosomal protein S6 kinase alpha-3 (chains A, B, C, D, E, F, G, H, I, J)
PQTEEVSIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAM
KVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRL
SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI
DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTM
ILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNKLYRRE
IHPPFKPATGRPEDTFYFDP
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| A1LU8 | 2,6-bis(fluoranyl)-4-[4-(4-morpholin-4-ylphenyl)pyridin-3-yl]phenol | C21 H18 F2 N2 O2 | 10 |
Primary citation
The Crystal Structure of RSK2 from Biortus. Wang, F., Cheng, W., Lv, Z. et al. To be published.
Other PDB entries of the same protein (UniProt P51812 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4NW6 1.74 Å, Rsk2 N-terminal kinase in complex with 2-amino-7-substituted benzoxazole compound 27
- 8EQ5 1.8 Å, Crystal structure of the N-terminal kinase domain of RSK2 in complex with SPRED2 (131-160)
- 4NW5 1.94 Å, Rsk2 N-terminal kinase in complex with 2-amino-7-substituted benzoxazole compound 8
- 5D9L 2.15 Å, Rsk2 N-terminal Kinase in Complex with bis-phenol pyrazole
- 8R58 2.31 Å, The RSK 2 N-terminal kinase domain in complex with BMF (1-19)
- 4NUS 2.39 Å, Rsk2 N-terminal kinase in complex with LJH685
- 4D9T 2.4 Å, Rsk2 C-terminal Kinase Domain with inhibitor (E)-methyl…
- 4D9U 2.4 Å, Rsk2 C-terminal Kinase Domain, (E)-tert-butyl 3-(4-amino-7-(3-hydroxypropyl)-5-p-tolyl-7H…
- 5D9K 2.55 Å, Rsk2 N-terminal Kinase in Complex with BI-D1870
- 4JG6 2.6 Å, RSK2 CTD bound to 2-cyano-3-(1H-indazol-5-yl)acrylamide
- 8XEY 2.65 Å, The Crystal Structure of C-terminal kinase domain of RSK2 from Biortus
- 7OPO 2.75 Å, RSK2 N-terminal kinase domain in complex with ORF45
Browse structure collections
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