6HYQ
Regulatory subunit of a cAMP-independent protein kinase A from Trypanosoma cruzi bound to guanosine
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue GMP A 601 |
Chain | Residue |
A | MET272 |
A | GLU312 |
A | VAL320 |
A | ALA321 |
A | TYR371 |
A | ILE292 |
A | TYR300 |
A | LYS302 |
A | ALA307 |
A | VAL308 |
A | GLY309 |
A | GLU310 |
A | LEU311 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue GMP A 602 |
Chain | Residue |
A | VAL411 |
A | CYS424 |
A | PHE426 |
A | ILE432 |
A | GLY433 |
A | GLU434 |
A | LEU435 |
A | GLU436 |
A | VAL444 |
A | ALA445 |
A | VAL447 |
A | LYS482 |
A | TYR483 |
A | TYR485 |
A | TYR486 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue GMP B 601 |
Chain | Residue |
B | MET272 |
B | ILE292 |
B | LYS294 |
B | TYR300 |
B | LYS302 |
B | ALA307 |
B | VAL308 |
B | GLY309 |
B | GLU310 |
B | LEU311 |
B | GLU312 |
B | VAL319 |
B | VAL320 |
B | ALA321 |
B | TYR371 |
B | HOH703 |
site_id | AC4 |
Number of Residues | 17 |
Details | binding site for residue GMP B 602 |
Chain | Residue |
B | VAL411 |
B | VAL423 |
B | CYS424 |
B | PHE426 |
B | ILE432 |
B | GLY433 |
B | GLU434 |
B | LEU435 |
B | GLU436 |
B | VAL444 |
B | ALA445 |
B | VAL447 |
B | LYS482 |
B | TYR483 |
B | TYR485 |
B | TYR486 |
B | HOH713 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ACT B 603 |
Chain | Residue |
B | GLU397 |
B | TYR499 |
B | VAL500 |
B | ASP501 |
site_id | AC6 |
Number of Residues | 13 |
Details | binding site for residue GMP C 601 |
Chain | Residue |
C | ILE292 |
C | LYS294 |
C | TYR300 |
C | LYS302 |
C | ALA307 |
C | VAL308 |
C | GLY309 |
C | GLU310 |
C | LEU311 |
C | GLU312 |
C | VAL320 |
C | ALA321 |
C | TYR371 |
site_id | AC7 |
Number of Residues | 16 |
Details | binding site for residue GMP C 602 |
Chain | Residue |
C | VAL411 |
C | VAL423 |
C | CYS424 |
C | PHE426 |
C | ILE432 |
C | GLY433 |
C | GLU434 |
C | LEU435 |
C | GLU436 |
C | VAL444 |
C | ALA445 |
C | VAL447 |
C | LYS482 |
C | TYR483 |
C | TYR485 |
C | TYR486 |
site_id | AC8 |
Number of Residues | 15 |
Details | binding site for residue GMP D 601 |
Chain | Residue |
D | ALA307 |
D | VAL308 |
D | GLY309 |
D | GLU310 |
D | LEU311 |
D | GLU312 |
D | VAL320 |
D | ALA321 |
D | TYR371 |
D | HOH730 |
D | MET272 |
D | ILE292 |
D | LYS294 |
D | TYR300 |
D | LYS302 |
site_id | AC9 |
Number of Residues | 17 |
Details | binding site for residue GMP D 602 |
Chain | Residue |
D | VAL411 |
D | VAL423 |
D | CYS424 |
D | PHE426 |
D | ILE432 |
D | GLY433 |
D | GLU434 |
D | LEU435 |
D | GLU436 |
D | VAL444 |
D | ALA445 |
D | VAL447 |
D | LYS482 |
D | TYR483 |
D | TYR485 |
D | TYR486 |
D | HOH707 |
Functional Information from PROSITE/UniProt
site_id | PS00888 |
Number of Residues | 17 |
Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. IIhYGEeGEwLYIImeG |
Chain | Residue | Details |
A | ILE391-GLY407 |