Hydrolysis of ATP in the crystal of Y204A mutant of cAMP-dependent protein kinase. Determined by X-ray diffraction at 1.26 Å resolution. Released 13 Apr 2004.
Explore 1RDQ in 3D Show helices and sheets RCSB PDB PDBe
1RDQ contains 18 α-helices and 15 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-31 | 17 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-51 | 9 | 1 |
| β-strand | 56-62 | 7 | 1 |
| β-strand | 68-75 | 8 | 1 |
| α-helix | 76-81 | 6 | |
| α-helix | 85-95 | 11 | |
| β-strand | 103 | 1 | 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 |
| β-strand | 199-200 | 2 | 5 |
| 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 | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 311-312 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 506-511 | 6 | |
| α-helix | 518-521 | 4 | |
| β-strand | 522-523 | 2 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cAMP-dependent protein kinase, alpha-catalytic subunit | E | protein | 350 | Mus musculus | P05132 (AlphaFold model) |
| cAMP-dependent protein kinase inhibitor, alpha form | I | protein | 20 |
>1RDQ_1 cAMP-dependent protein kinase, alpha-catalytic subunit (chains E) GNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLV KHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVM EYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI QVTDFGFAKRVKGRTWTLCGTPEALAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATT DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
>1RDQ_2 cAMP-dependent protein kinase inhibitor, alpha form (chains I) TTYADFIASGRTGRRNAIHD
| ID | Name | Formula | Copies |
|---|---|---|---|
| MRD | (4R)-2-methylpentane-2,4-diol | C6 H14 O2 | 1 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| MG | Magnesium ion | Mg | 2 |
| PO4 | Phosphate ion | O4 P | 1 |
Water and common crystallization additives (GOL) are not listed.
Crystal Structure of a cAMP-dependent Protein Kinase Mutant at 1.26A: New Insights into the Catalytic Mechanism. Yang, J., Ten Eyck, L.F., Xuong, N.H. et al. J Mol Biol (2004) 336:473-487. DOI 10.1016/j.jmb.2003.11.044 · PubMed
Other PDB entries of the same protein (UniProt P05132 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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