3E8E: Kinase domain of PKA
Crystal structures of the kinase domain of PKA in complex with ATP-competitive inhibitors. Determined by X-ray diffraction at 2.0 Å resolution. Released 18 Nov 2008.
- Method
- X-ray diffraction
- Resolution
- 2.0 Å
- Organism
- Bos taurus
- Chains
- 12
- Atoms
- 18,474
- Mol. weight
- 260.86 kDa
- Ligands
- G98
- Released
- 18 Nov 2008
Explore 3E8E in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3E8E contains 121 α-helices and 79 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: 18 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-31 | 21 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-51 | 9 | 1 |
| β-strand | 55-62 | 8 | 1 |
| β-strand | 68-75 | 8 | 1 |
| α-helix | 76-81 | 6 | |
| α-helix | 85-97 | 13 | |
| β-strand | 103 | 1 | 2 |
| α-helix | 104-105 | 2 | |
| β-strand | 106-111 | 6 | 1 |
| β-strand | 115-121 | 7 | 1 |
| β-strand | 127 | 1 | 2 |
| α-helix | 128-135 | 8 | |
| α-helix | 140-159 | 20 | |
| β-strand | 162-163 | 2 | 3 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 2 |
| β-strand | 180-182 | 3 | 2 |
| β-strand | 189-190 | 2 | 3 |
| β-strand | 195 | 1 | 4 |
| α-helix | 202-204 | 3 | |
| α-helix | 207-210 | 4 | |
| β-strand | 215 | 1 | 4 |
| α-helix | 218-233 | 16 | |
| α-helix | 243-252 | 10 | |
| α-helix | 263-272 | 10 | |
| α-helix | 277-279 | 3 | |
| α-helix | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 311-312 | 2 | |
Chain B: 19 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-31 | 19 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-51 | 9 | 5 |
| β-strand | 55-62 | 8 | 5 |
| β-strand | 68-75 | 8 | 5 |
| α-helix | 76-81 | 6 | |
| α-helix | 85-97 | 13 | |
| β-strand | 103 | 1 | 6 |
| α-helix | 104-105 | 2 | |
| β-strand | 106-111 | 6 | 5 |
| β-strand | 115-120 | 6 | 5 |
| β-strand | 127 | 1 | 6 |
| α-helix | 128-135 | 8 | |
| α-helix | 140-159 | 20 | |
| β-strand | 162-163 | 2 | 7 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 6 |
| β-strand | 180-182 | 3 | 6 |
| β-strand | 189-190 | 2 | 7 |
| β-strand | 195 | 1 | 8 |
| α-helix | 202-204 | 3 | |
| α-helix | 207-210 | 4 | |
| β-strand | 215 | 1 | 8 |
| α-helix | 218-233 | 16 | |
| α-helix | 243-252 | 10 | |
| α-helix | 263-272 | 10 | |
| α-helix | 277-279 | 3 | |
| α-helix | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 311-312 | 2 | |
| α-helix | 341-342 | 2 | |
Chains C, G and J: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-12 | 7 | |
| α-helix | 18-21 | 4 | |
Chain E: 20 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-10 | 3 | |
| α-helix | 11-31 | 21 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-51 | 9 | 9 |
| β-strand | 55-62 | 8 | 9 |
| β-strand | 68-75 | 8 | 9 |
| α-helix | 76-81 | 6 | |
| α-helix | 85-97 | 13 | |
| β-strand | 103 | 1 | 10 |
| α-helix | 104-105 | 2 | |
| β-strand | 106-111 | 6 | 9 |
| β-strand | 115-120 | 6 | 9 |
| β-strand | 127 | 1 | 10 |
| α-helix | 128-135 | 8 | |
| α-helix | 140-159 | 20 | |
| β-strand | 162-163 | 2 | 11 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 10 |
| β-strand | 180-182 | 3 | 10 |
| β-strand | 189-190 | 2 | 11 |
| β-strand | 195 | 1 | 12 |
| α-helix | 202-204 | 3 | |
| α-helix | 207-210 | 4 | |
| β-strand | 215 | 1 | 12 |
| α-helix | 218-233 | 16 | |
| α-helix | 243-252 | 10 | |
| α-helix | 263-272 | 10 | |
| α-helix | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 311-312 | 2 | |
| α-helix | 316-318 | 3 | |
| α-helix | 336-338 | 3 | |
Chains F and N: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-12 | 7 | |
Chain I: 20 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-8 | 5 | |
| α-helix | 11-31 | 21 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-52 | 10 | 13 |
| β-strand | 55-62 | 8 | 13 |
| β-strand | 68-75 | 8 | 13 |
| α-helix | 76-81 | 6 | |
| α-helix | 85-97 | 13 | |
| β-strand | 103 | 1 | 14 |
| α-helix | 104-105 | 2 | |
| β-strand | 106-111 | 6 | 13 |
| β-strand | 115-121 | 7 | 13 |
| β-strand | 127 | 1 | 14 |
| α-helix | 128-135 | 8 | |
| α-helix | 140-159 | 20 | |
| β-strand | 162-163 | 2 | 15 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 14 |
| β-strand | 180-182 | 3 | 14 |
| β-strand | 189-190 | 2 | 15 |
| β-strand | 195 | 1 | 16 |
| α-helix | 202-204 | 3 | |
| α-helix | 207-210 | 4 | |
| β-strand | 215 | 1 | 16 |
| α-helix | 218-233 | 16 | |
| α-helix | 243-252 | 10 | |
| α-helix | 263-272 | 10 | |
| α-helix | 277-279 | 3 | |
| α-helix | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 311-312 | 2 | |
| α-helix | 316-318 | 3 | |
Chain L: 17 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14-31 | 18 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-51 | 9 | 17 |
| β-strand | 55-62 | 8 | 17 |
| β-strand | 68-75 | 8 | 17 |
| α-helix | 76-81 | 6 | |
| α-helix | 85-97 | 13 | |
| β-strand | 103 | 1 | 18 |
| α-helix | 104-105 | 2 | |
| β-strand | 106-111 | 6 | 17 |
| β-strand | 115-121 | 7 | 17 |
| β-strand | 127 | 1 | 18 |
| α-helix | 128-135 | 8 | |
| α-helix | 140-159 | 20 | |
| β-strand | 162-163 | 2 | 19 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 18 |
| β-strand | 180-182 | 3 | 18 |
| β-strand | 189-190 | 2 | 19 |
| β-strand | 195 | 1 | 20 |
| α-helix | 202-204 | 3 | |
| α-helix | 207-210 | 4 | |
| β-strand | 215 | 1 | 20 |
| α-helix | 218-233 | 16 | |
| α-helix | 243-252 | 10 | |
| α-helix | 263-272 | 10 | |
| α-helix | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 311-312 | 2 | |
Chain P: 17 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-31 | 22 | |
| β-strand | 36 | 1 | 21 |
| α-helix | 40-42 | 3 | |
| β-strand | 43-51 | 9 | 21 |
| β-strand | 55-62 | 8 | 21 |
| β-strand | 68-75 | 8 | 21 |
| α-helix | 76-81 | 6 | |
| α-helix | 85-97 | 13 | |
| β-strand | 103 | 1 | 22 |
| α-helix | 104-105 | 2 | |
| β-strand | 106-111 | 6 | 21 |
| β-strand | 115-120 | 6 | 21 |
| β-strand | 127 | 1 | 22 |
| α-helix | 128-135 | 8 | |
| α-helix | 140-159 | 20 | |
| β-strand | 162-163 | 2 | 23 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 22 |
| β-strand | 180-182 | 3 | 22 |
| β-strand | 189-190 | 2 | 23 |
| β-strand | 195 | 1 | 24 |
| α-helix | 202-204 | 3 | |
| α-helix | 207-210 | 4 | |
| β-strand | 215 | 1 | 24 |
| α-helix | 218-233 | 16 | |
| α-helix | 243-252 | 10 | |
| α-helix | 263-272 | 10 | |
| α-helix | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 311-312 | 2 | |
1 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 |
|---|
| cAMP-dependent protein kinase catalytic subunit alpha | A, B, E, I, L, P | protein | 350 | Bos taurus | P00517 (AlphaFold model) |
| PKI inhibitor peptide | C, F, G, J, N, Q | protein | 20 | | Q3SX13 (AlphaFold model) |
Sequence of entity 1 (A, B, E, I, L, P), FASTA
>3E8E_1 cAMP-dependent protein kinase catalytic subunit alpha (chains A, B, E, I, L, P)
GNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLV
KHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVM
EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI
QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA
DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATT
DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Sequence of entity 2 (C, F, G, J, N, Q), FASTA
>3E8E_2 PKI inhibitor peptide (chains C, F, G, J, N, Q)
TTYADFIASGRTGRRNAIHD
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| G98 | 4-[2-(4-amino-2,5-dihydro-1,2,5-oxadiazol-3-yl)-6-{[(1S)-3-amino-1-phenylpropyl… | C24 H29 N7 O3 | 6 |
Primary citation
Aminofurazans as potent inhibitors of AKT kinase. Rouse, M.B., Seefeld, M.A., Leber, J.D. et al. Bioorg Med Chem Lett (2009) 19:1508-1511. DOI 10.1016/j.bmcl.2009.01.002 · PubMed
Other PDB entries of the same protein (UniProt P00517 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4Z84 1.55 Å, PKAB3 in complex with pyrrolidine inhibitor 34a
- 4C38 1.58 Å, PKA-S6K1 Chimera with compound 21e (CCT239066) bound
- 1XH8 1.6 Å, Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein…
- 5VHB 1.61 Å, Crystal structure of Protein Kinase A in complex with the PKI peptide and…
- 1XH9 1.64 Å, Crystal Structures of Protein Kinase B Selective Inhibitors in Complex with Protein…
- 3ZO4 1.65 Å, The Synthesis and Evaluation of Diazaspirocyclic Protein Kinase Inhibitors
- 4C33 1.7 Å, PKA-S6K1 Chimera Apo
- 4C37 1.7 Å, PKA-S6K1 Chimera with compound 21a (CCT196539) bound
- 8SF8 1.7 Å, Structure of bovine PKA bound to (R)-N-(4-(1H-pyrrolo[2,3-b]pyridin-4-yl)phenyl)-2-amino-…
- 4C34 1.78 Å, PKA-S6K1 Chimera with Staurosporine bound
- 3KKV 1.8 Å, Structure of PKA with a protein Kinase B-selective inhibitor.
- 4Z83 1.8 Å, PKAB3 in complex with pyrrolidine inhibitor 47a
Browse structure collections
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