Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0010506 | biological_process | regulation of autophagy |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
B | 0010506 | biological_process | regulation of autophagy |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004674 | molecular_function | protein serine/threonine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
C | 0010506 | biological_process | regulation of autophagy |
D | 0004672 | molecular_function | protein kinase activity |
D | 0004674 | molecular_function | protein serine/threonine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
D | 0010506 | biological_process | regulation of autophagy |
E | 0004672 | molecular_function | protein kinase activity |
E | 0004674 | molecular_function | protein serine/threonine kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006468 | biological_process | protein phosphorylation |
E | 0010506 | biological_process | regulation of autophagy |
F | 0004672 | molecular_function | protein kinase activity |
F | 0004674 | molecular_function | protein serine/threonine kinase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006468 | biological_process | protein phosphorylation |
F | 0010506 | biological_process | regulation of autophagy |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ANP A 300 |
Chain | Residue |
A | LEU16 |
A | LYS39 |
A | MET87 |
A | GLU88 |
A | TYR89 |
A | ILE90 |
A | LEU140 |
A | PHE150 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BEN A 301 |
Chain | Residue |
A | GLN64 |
A | LEU65 |
A | SER66 |
A | MET73 |
C | GLU88 |
A | SER63 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ANP B 300 |
Chain | Residue |
B | LEU16 |
B | GLY18 |
B | LYS39 |
B | GLU88 |
B | TYR89 |
B | ILE90 |
B | LEU140 |
B | PHE150 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BEN B 301 |
Chain | Residue |
B | SER63 |
B | LEU65 |
B | SER66 |
B | MET73 |
B | GLU88 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ANP C 300 |
Chain | Residue |
C | LEU16 |
C | GLY18 |
C | LYS39 |
C | GLU88 |
C | TYR89 |
C | ILE90 |
C | LEU140 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BEN C 301 |
Chain | Residue |
A | GLU88 |
C | SER63 |
C | GLN64 |
C | LEU65 |
C | SER66 |
C | MET73 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ANP D 300 |
Chain | Residue |
D | SER22 |
D | VAL24 |
D | GLU88 |
D | TYR89 |
D | ILE90 |
D | LEU140 |
D | PHE150 |
D | ASP151 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ANP E 300 |
Chain | Residue |
E | VAL24 |
E | LYS39 |
E | GLU88 |
E | TYR89 |
E | ILE90 |
E | LYS135 |
E | LEU140 |
E | PHE150 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ANP F 300 |
Chain | Residue |
F | VAL24 |
F | LYS39 |
F | GLU88 |
F | TYR89 |
F | ILE90 |
F | LYS135 |
F | LEU140 |
F | PHE150 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGGMSTVYlAedtilnik..........VAIK |
Chain | Residue | Details |
A | LEU16-LYS39 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKpqNILI |
Chain | Residue | Details |
A | ILE129-ILE141 | |