7LZ4
Crystal structure of A211D mutant of Protein Kinase A RIa subunit, a Carney Complex mutation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001932 | biological_process | regulation of protein phosphorylation |
A | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
A | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
B | 0001932 | biological_process | regulation of protein phosphorylation |
B | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
B | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
C | 0001932 | biological_process | regulation of protein phosphorylation |
C | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
C | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
D | 0001932 | biological_process | regulation of protein phosphorylation |
D | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
D | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
E | 0001932 | biological_process | regulation of protein phosphorylation |
E | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
E | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
F | 0001932 | biological_process | regulation of protein phosphorylation |
F | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
F | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
G | 0001932 | biological_process | regulation of protein phosphorylation |
G | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
G | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
H | 0001932 | biological_process | regulation of protein phosphorylation |
H | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
H | 0008603 | molecular_function | cAMP-dependent protein kinase regulator activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue CMP A 401 |
Chain | Residue |
A | PHE198 |
A | GLY199 |
A | GLU200 |
A | LEU201 |
A | ALA202 |
A | ARG209 |
A | ALA210 |
A | ASP211 |
A | TRP260 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue CMP A 402 |
Chain | Residue |
A | VAL300 |
A | GLN302 |
A | VAL313 |
A | PHE322 |
A | GLY323 |
A | GLU324 |
A | ILE325 |
A | ARG333 |
A | ALA334 |
A | ALA335 |
A | TYR371 |
A | ASN372 |
A | SER373 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue CMP B 401 |
Chain | Residue |
B | PHE198 |
B | GLY199 |
B | GLU200 |
B | LEU201 |
B | ALA202 |
B | ARG209 |
B | ALA210 |
B | ASP211 |
B | TRP260 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue CMP B 402 |
Chain | Residue |
B | VAL300 |
B | GLN302 |
B | VAL313 |
B | GLY323 |
B | GLU324 |
B | ILE325 |
B | ALA326 |
B | PRO332 |
B | ARG333 |
B | ALA334 |
B | ALA335 |
B | TYR371 |
B | ASN372 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue CMP C 401 |
Chain | Residue |
C | PHE198 |
C | GLY199 |
C | GLU200 |
C | LEU201 |
C | ALA202 |
C | ARG209 |
C | ALA210 |
C | ASP211 |
C | TRP260 |
site_id | AC6 |
Number of Residues | 14 |
Details | binding site for residue CMP C 402 |
Chain | Residue |
C | VAL281 |
C | VAL300 |
C | VAL313 |
C | PHE322 |
C | GLY323 |
C | GLU324 |
C | ILE325 |
C | ALA326 |
C | ARG333 |
C | ALA334 |
C | ALA335 |
C | TYR371 |
C | ASN372 |
C | SER373 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue CMP D 401 |
Chain | Residue |
D | PHE198 |
D | GLY199 |
D | GLU200 |
D | LEU201 |
D | ALA202 |
D | ARG209 |
D | ALA210 |
D | ASP211 |
D | TRP260 |
site_id | AC8 |
Number of Residues | 14 |
Details | binding site for residue CMP D 402 |
Chain | Residue |
D | GLN302 |
D | VAL313 |
D | PHE322 |
D | GLY323 |
D | GLU324 |
D | ILE325 |
D | ALA326 |
D | PRO332 |
D | ARG333 |
D | ALA334 |
D | ALA335 |
D | TYR371 |
D | ASN372 |
D | SER373 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue CMP E 401 |
Chain | Residue |
E | PHE198 |
E | GLY199 |
E | GLU200 |
E | LEU201 |
E | ALA202 |
E | ARG209 |
E | ALA210 |
E | ASP211 |
E | TRP260 |
site_id | AD1 |
Number of Residues | 13 |
Details | binding site for residue CMP E 402 |
Chain | Residue |
E | VAL300 |
E | VAL313 |
E | PHE322 |
E | GLY323 |
E | GLU324 |
E | ILE325 |
E | ALA326 |
E | ARG333 |
E | ALA334 |
E | ALA335 |
E | VAL337 |
E | TYR371 |
E | ASN372 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue CMP F 401 |
Chain | Residue |
F | PHE198 |
F | GLY199 |
F | GLU200 |
F | LEU201 |
F | ALA202 |
F | ARG209 |
F | ALA210 |
F | ASP211 |
F | TRP260 |
site_id | AD3 |
Number of Residues | 14 |
Details | binding site for residue CMP F 402 |
Chain | Residue |
F | VAL300 |
F | GLN302 |
F | VAL313 |
F | PHE322 |
F | GLY323 |
F | GLU324 |
F | ILE325 |
F | ALA326 |
F | ARG333 |
F | ALA334 |
F | ALA335 |
F | VAL337 |
F | TYR371 |
F | ASN372 |
site_id | AD4 |
Number of Residues | 10 |
Details | binding site for residue CMP G 401 |
Chain | Residue |
G | PHE198 |
G | GLY199 |
G | GLU200 |
G | LEU201 |
G | ALA202 |
G | ARG209 |
G | ALA210 |
G | ASP211 |
G | LYS259 |
G | TRP260 |
site_id | AD5 |
Number of Residues | 11 |
Details | binding site for residue CMP G 402 |
Chain | Residue |
G | VAL313 |
G | PHE322 |
G | GLY323 |
G | GLU324 |
G | ALA326 |
G | ARG333 |
G | ALA334 |
G | ALA335 |
G | TYR371 |
G | ASN372 |
G | SER373 |
site_id | AD6 |
Number of Residues | 10 |
Details | binding site for residue CMP H 401 |
Chain | Residue |
H | PHE198 |
H | GLY199 |
H | GLU200 |
H | LEU201 |
H | ALA202 |
H | ARG209 |
H | ALA210 |
H | ASP211 |
H | LYS259 |
H | TRP260 |
site_id | AD7 |
Number of Residues | 14 |
Details | binding site for residue CMP H 402 |
Chain | Residue |
H | VAL281 |
H | VAL300 |
H | VAL313 |
H | PHE322 |
H | GLY323 |
H | GLU324 |
H | ILE325 |
H | ALA326 |
H | ARG333 |
H | ALA334 |
H | ALA335 |
H | VAL337 |
H | TYR371 |
H | ASN372 |
Functional Information from PROSITE/UniProt
site_id | PS00888 |
Number of Residues | 17 |
Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VIqQGDeGDnFYVIdqG |
Chain | Residue | Details |
A | VAL162-GLY178 | |
A | ILE280-GLY296 |
site_id | PS00889 |
Number of Residues | 18 |
Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEiALlmnrp......RAAtVvA |
Chain | Residue | Details |
A | PHE322-ALA339 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 48 |
Details | BINDING: |
Chain | Residue | Details |
A | LEU135 | |
B | ILE253 | |
B | GLU324 | |
B | ARG333 | |
C | LEU135 | |
C | GLU200 | |
C | ARG209 | |
C | ILE253 | |
C | GLU324 | |
C | ARG333 | |
D | LEU135 | |
A | GLU200 | |
D | GLU200 | |
D | ARG209 | |
D | ILE253 | |
D | GLU324 | |
D | ARG333 | |
E | LEU135 | |
E | GLU200 | |
E | ARG209 | |
E | ILE253 | |
E | GLU324 | |
A | ARG209 | |
E | ARG333 | |
F | LEU135 | |
F | GLU200 | |
F | ARG209 | |
F | ILE253 | |
F | GLU324 | |
F | ARG333 | |
G | LEU135 | |
G | GLU200 | |
G | ARG209 | |
A | ILE253 | |
G | ILE253 | |
G | GLU324 | |
G | ARG333 | |
H | LEU135 | |
H | GLU200 | |
H | ARG209 | |
H | ILE253 | |
H | GLU324 | |
H | ARG333 | |
A | GLU324 | |
A | ARG333 | |
B | LEU135 | |
B | GLU200 | |
B | ARG209 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09456 |
Chain | Residue | Details |
A | SER256 | |
B | SER256 | |
C | SER256 | |
D | SER256 | |
E | SER256 | |
F | SER256 | |
G | SER256 | |
H | SER256 |