7OPO: RSK2 N-terminal kinase domain
RSK2 N-terminal kinase domain in complex with ORF45. Determined by X-ray diffraction at 2.75 Å resolution. Released 2 Feb 2022.
- Method
- X-ray diffraction
- Resolution
- 2.75 Å
- Organisms
- Homo sapiens, Human herpesvirus 8
- Chains
- 12
- Atoms
- 16,458
- Mol. weight
- 261.22 kDa
- Ligands
- ANP
- Released
- 2 Feb 2022
Explore 7OPO in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7OPO contains 113 α-helices and 123 β-strands across 12 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: 17 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 47-51 | 5 | 1 |
| β-strand | 55 | 1 | 2 |
| α-helix | 61-63 | 3 | |
| α-helix | 65-67 | 3 | |
| β-strand | 68-77 | 10 | 2 |
| β-strand | 80-87 | 8 | 2 |
| β-strand | 96-102 | 7 | 2 |
| β-strand | 104-110 | 7 | 1 |
| α-helix | 121-124 | 4 | |
| β-strand | 127 | 1 | 3 |
| β-strand | 130 | 1 | 3 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-139 | 7 | 2 |
| β-strand | 142-148 | 7 | 2 |
| β-strand | 153-154 | 2 | 3 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-186 | 20 | |
| α-helix | 196-198 | 3 | |
| β-strand | 199-201 | 3 | 3 |
| β-strand | 207-209 | 3 | 3 |
| β-strand | 214-217 | 4 | 1 |
| β-strand | 224 | 1 | 4 |
| α-helix | 232-234 | 3 | |
| α-helix | 237-240 | 4 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-282 | 10 | |
| β-strand | 284-285 | 2 | 5 |
| α-helix | 286-288 | 3 | |
| α-helix | 293-302 | 10 | |
| β-strand | 304 | 1 | 6 |
| α-helix | 307-309 | 3 | |
| α-helix | 318-322 | 5 | |
| α-helix | 326-329 | 4 | |
| α-helix | 332-336 | 5 | |
Chains B and D: 3 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 24-29 | 6 | |
| α-helix | 36-38 | 3 | |
| β-strand | 46 | 1 | 7 |
| β-strand | 56-58 | 3 | 5 |
| β-strand | 64 | 1 | 6 |
| β-strand | 66 | 1 | 5 |
| α-helix | 67-68 | 2 | |
Chain C: 16 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 47-51 | 5 | 8 |
| β-strand | 55-56 | 2 | 7 |
| α-helix | 65-67 | 3 | |
| β-strand | 68-77 | 10 | 7 |
| β-strand | 80-87 | 8 | 7 |
| β-strand | 96-102 | 7 | 7 |
| β-strand | 104-110 | 7 | 8 |
| α-helix | 121-124 | 4 | |
| β-strand | 127 | 1 | 9 |
| β-strand | 130 | 1 | 9 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-139 | 7 | 7 |
| β-strand | 142-148 | 7 | 7 |
| β-strand | 153-154 | 2 | 9 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-186 | 20 | |
| α-helix | 196-198 | 3 | |
| β-strand | 199-201 | 3 | 9 |
| β-strand | 207-209 | 3 | 9 |
| β-strand | 214-217 | 4 | 8 |
| β-strand | 224 | 1 | 4 |
| α-helix | 232-234 | 3 | |
| α-helix | 237-241 | 5 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-282 | 10 | |
| β-strand | 284-285 | 2 | 10 |
| α-helix | 286-288 | 3 | |
| α-helix | 293-302 | 10 | |
| β-strand | 304 | 1 | 11 |
| α-helix | 307-309 | 3 | |
| α-helix | 318-322 | 5 | |
| α-helix | 326-329 | 4 | |
| α-helix | 332-336 | 5 | |
Chain E: 16 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 48-51 | 4 | 12 |
| β-strand | 55-56 | 2 | 13 |
| α-helix | 65-67 | 3 | |
| β-strand | 68-77 | 10 | 13 |
| β-strand | 80-87 | 8 | 13 |
| β-strand | 96-102 | 7 | 13 |
| β-strand | 104-109 | 6 | 12 |
| α-helix | 121-124 | 4 | |
| β-strand | 130 | 1 | 14 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-139 | 7 | 13 |
| β-strand | 142-148 | 7 | 13 |
| β-strand | 153-154 | 2 | 14 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-186 | 20 | |
| α-helix | 196-198 | 3 | |
| β-strand | 199-201 | 3 | 14 |
| β-strand | 207-209 | 3 | 14 |
| β-strand | 214-217 | 4 | 12 |
| β-strand | 224 | 1 | 15 |
| α-helix | 232-234 | 3 | |
| α-helix | 237-241 | 5 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-282 | 10 | |
| β-strand | 284-285 | 2 | 16 |
| α-helix | 286-288 | 3 | |
| α-helix | 293-302 | 10 | |
| β-strand | 304 | 1 | 17 |
| α-helix | 307-309 | 3 | |
| α-helix | 318-322 | 5 | |
| α-helix | 325-329 | 5 | |
| α-helix | 332-336 | 5 | |
Chain F: 4 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 36-38 | 3 | |
| α-helix | 45 | 1 | |
| β-strand | 46 | 1 | 18 |
| α-helix | 47-48 | 2 | |
| β-strand | 56-58 | 3 | 16 |
| β-strand | 64 | 1 | 17 |
| β-strand | 66 | 1 | 16 |
| α-helix | 67-68 | 2 | |
Chain G: 15 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 48-51 | 4 | 19 |
| β-strand | 55 | 1 | 18 |
| α-helix | 65-67 | 3 | |
| β-strand | 68-77 | 10 | 18 |
| β-strand | 80-87 | 8 | 18 |
| β-strand | 96-102 | 7 | 18 |
| β-strand | 104-109 | 6 | 19 |
| α-helix | 118-124 | 7 | |
| β-strand | 127 | 1 | 20 |
| β-strand | 130 | 1 | 20 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-139 | 7 | 18 |
| β-strand | 142-148 | 7 | 18 |
| β-strand | 153-154 | 2 | 20 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-186 | 20 | |
| α-helix | 196-198 | 3 | |
| β-strand | 199-201 | 3 | 20 |
| β-strand | 207-209 | 3 | 20 |
| β-strand | 214-217 | 4 | 19 |
| β-strand | 224 | 1 | 15 |
| α-helix | 237-240 | 4 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-282 | 10 | |
| β-strand | 284-286 | 3 | 21 |
| α-helix | 287-288 | 2 | |
| α-helix | 293-302 | 10 | |
| β-strand | 304 | 1 | 22 |
| α-helix | 307-309 | 3 | |
| α-helix | 318-322 | 5 | |
| α-helix | 325-327 | 3 | |
| α-helix | 332-336 | 5 | |
Chain H: 3 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 24-26 | 3 | |
| α-helix | 36-38 | 3 | |
| β-strand | 46 | 1 | 13 |
| β-strand | 56-58 | 3 | 21 |
| β-strand | 64 | 1 | 22 |
| β-strand | 66-67 | 2 | 21 |
| α-helix | 68-69 | 2 | |
Chain I: 14 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 47-52 | 6 | 23 |
| β-strand | 55-56 | 2 | 24 |
| α-helix | 65-67 | 3 | |
| β-strand | 68-77 | 10 | 24 |
| β-strand | 80-87 | 8 | 24 |
| β-strand | 96-102 | 7 | 24 |
| β-strand | 104-110 | 7 | 23 |
| α-helix | 121-124 | 4 | |
| β-strand | 127 | 1 | 25 |
| β-strand | 130 | 1 | 25 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-139 | 7 | 24 |
| β-strand | 142-148 | 7 | 24 |
| β-strand | 153-154 | 2 | 25 |
| α-helix | 155-162 | 8 | |
| α-helix | 167-186 | 20 | |
| α-helix | 196-198 | 3 | |
| β-strand | 199-201 | 3 | 25 |
| β-strand | 207-209 | 3 | 25 |
| β-strand | 214-217 | 4 | 23 |
| β-strand | 224 | 1 | 26 |
| α-helix | 237-240 | 4 | |
| α-helix | 247-263 | 17 | |
| α-helix | 273-282 | 10 | |
| β-strand | 284-285 | 2 | 27 |
| α-helix | 286-288 | 3 | |
| α-helix | 293-302 | 10 | |
| β-strand | 304 | 1 | 28 |
| α-helix | 318-322 | 5 | |
| α-helix | 326-329 | 4 | |
| α-helix | 332-336 | 5 | |
3 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, C, E, G, I, K | protein | 317 | Homo sapiens | P51812 (AlphaFold model) |
| Protein ORF45 | B, D, F, H, J, L | protein | 63 | Human herpesvirus 8 | F5HDE4 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G, I, K), FASTA
>7OPO_1 Ribosomal protein S6 kinase alpha-3 (chains A, C, E, G, I, K)
GSASNPQTEEVSIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSDAR
QLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGD
LFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL
SKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRK
ETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNK
LYRREIHPPFKPATGRP
Sequence of entity 2 (B, D, F, H, J, L), FASTA
>7OPO_2 Protein ORF45 (chains B, D, F, H, J, L)
GSRMLPIEGAPRRRPPVKFIFPPPPLSSLPGFGRPRGYAGPTVIDMSAPDDVFAEDTPSP
PAT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 6 |
Primary citation
A non-catalytic herpesviral protein reconfigures ERK-RSK signaling by targeting kinase docking systems in the host. Alexa, A., Sok, P., Gross, F. et al. Nat Commun (2022) 13:472-472. DOI 10.1038/s41467-022-28109-x · PubMed
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
- 4JG7 3.0 Å, Structure of RSK2 CTD bound to 3-(3-(1H-pyrrolo[2,3-b]pyridine-3-carbonyl)phenyl)-2-cyano…
Browse structure collections
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