Turn motif phosphorylation regulates processing of cAMP-dependent protein kinase
Steichen, J.M., Yang, J., Taylor, S.S.To be published.
Experimental Data Snapshot
Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
cAMP-dependent protein kinase catalytic subunit alpha | A [auth E] | 371 | Mus musculus | Mutation(s): 1  Gene Names: Prkaca, Pkaca EC: 2.7.11.11 | |
UniProt | |||||
Find proteins for P05132 (Mus musculus) Explore P05132  Go to UniProtKB:  P05132 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P05132 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by: Sequence | 3D Structure
Entity ID: 2 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
cAMP-dependent protein kinase inhibitor alpha | B [auth A] | 20 | Mus musculus | Mutation(s): 0  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P63248 (Mus musculus) Explore P63248  Go to UniProtKB:  P63248 | |||||
IMPC:  MGI:104747 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P63248 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 2 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
ANP Query on ANP | C [auth E] | PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER C10 H17 N6 O12 P3 PVKSNHVPLWYQGJ-KQYNXXCUSA-N | |||
MG Query on MG | D [auth E], E | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |
Modified Residues 2 Unique | |||||
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ID | Chains | Type | Formula | 2D Diagram | Parent |
SEP Query on SEP | A [auth E] | L-PEPTIDE LINKING | C3 H8 N O6 P | SER | |
TPO Query on TPO | A [auth E] | L-PEPTIDE LINKING | C4 H10 N O6 P | THR |
Length ( ? ) | Angle ( ? ) |
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a = 72.29 | ¦Á = 90 |
b = 76.69 | ¦Â = 90 |
c = 80.31 | ¦Ă = 90 |
Software Name | Purpose |
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ADSC | data collection |
PHASER | phasing |
REFMAC | refinement |
MOSFLM | data reduction |
SCALA | data scaling |