DI1100031
cAMP-dependent protein kinase complexed with an unmodified PKI-alpha peptide
1apm
X-ray
2.00
Mus musculus
Inferred from homology
15299526
Knighton DR, Bell SM, Zheng J, Ten Eyck LF, Xuong NH, Taylor SS, Sowadski JM
2.0 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with a peptide inhibitor and detergent.
Acta Crystallogr. D Biol. Crystallogr.
1993
Pt 3
49
357-61
. A mutant (Serl39Ala) of the mouse recombinant catalytic (C) subunit of cAMP-dependent protein kinase was co-crystallized with a peptide inhibitor, PKI(5-24), and MEGA-8 (octanoyl-N-methylglucamide) detergent. This structure was refined using all observed data (30 248 reflections) between 30 and 1.95 A resolution to an R factor of 0.186. R.m.s. deviations of bond lengths and bond angles are 0.013 A and 2.3 degrees, respectively. The final model has 3075 atoms (207 solvent) with a mean B factor of 31.9 A(2). The placement of invariant protein-kinase residues and most C:PKI(5-24) interactions were confirmed, but register errors affecting residues 55-64 and 309-339 were corrected during refinement by shifting the affected sequences toward the C terminus along the previously determined backbone path. New details of C:PKI(5-24) interactions and the Ser338 autophosphorylation site are described, and the acyl group binding site near the catalytic subunit NH(2) terminus is identified.
GO:0019901
protein kinase binding
GO:0051018
protein kinase A binding
GO:0050794
regulation of cellular process
GO:0033157
regulation of intracellular protein transport
GO:0005634
nucleus
GO:0005737
cytoplasm
No modifications of the original PDB file.
The entry DI1100095 describes the same interaction with the disordered partner bearing different post-translational modification(s).
2
Protein kinase
I
cAMP-dependent protein kinase inhibitor alpha
Disordered
Mus musculus
TTYADFIASGRTGRRNAIHD
20
P63248
6
25
26.3%
UniRef90_P63248
6
25
secondary structure
helix
7
13
secondary structure
beta
23
23
pfam
PF02827.13
PKI
2
70
E
cAMP-dependent protein kinase catalytic subunit alpha
Ordered
Mus musculus
SEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
341
P05132
11
351
97.2%
UniRef90_P17612
11
351
secondary structure
helix
12
32
secondary structure
helix
41
43
secondary structure
beta
44
52
secondary structure
beta
56
63
secondary structure
beta
69
76
secondary structure
helix
77
82
secondary structure
helix
86
98
secondary structure
beta
104
104
secondary structure
beta
107
112
secondary structure
beta
116
122
secondary structure
beta
128
128
secondary structure
helix
129
136
secondary structure
helix
141
160
secondary structure
beta
163
164
secondary structure
helix
170
172
secondary structure
beta
173
175
secondary structure
beta
181
183
secondary structure
beta
190
191
secondary structure
beta
196
196
secondary structure
beta
201
201
secondary structure
helix
203
205
secondary structure
helix
208
211
secondary structure
beta
216
216
secondary structure
helix
219
234
secondary structure
helix
244
253
secondary structure
helix
264
273
secondary structure
helix
290
293
secondary structure
helix
296
298
secondary structure
helix
303
308
pfam
PF00069.22
Pkinase
44
298
I
The corresponding region of a closely homologous protein has been shown to be disordered in the 1-76 region described in DisProt entry DP00015 (covers 100% of the sequence present in the structure).
E
The protein kinase domain involved in the interaction is known to adopt a stable structure in isolation (see Pfam domain PF00069). A solved monomeric structure of the domain is represented by PDB ID 4nts.
1atp
2cpk
2gnf
2gng
2qur
3fjq
3ow3
3qal
3qam
4dfx
4dfz
4dg0
4dg2
4dg3
4dh1
4dh3
4dh5
4dh7
4dh8
1l3r
1q8u
1svh
1yds
1ydt