8AHT
Crystal structure of Plasmodium falciparum Ca2+/Calmodulin in complex with melittin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0008047 | molecular_function | enzyme activator activity |
A | 0020007 | cellular_component | apical complex |
A | 0046872 | molecular_function | metal ion binding |
A | 0061891 | molecular_function | calcium ion sensor activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0008047 | molecular_function | enzyme activator activity |
B | 0020007 | cellular_component | apical complex |
B | 0046872 | molecular_function | metal ion binding |
B | 0061891 | molecular_function | calcium ion sensor activity |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0008047 | molecular_function | enzyme activator activity |
C | 0020007 | cellular_component | apical complex |
C | 0046872 | molecular_function | metal ion binding |
C | 0061891 | molecular_function | calcium ion sensor activity |
D | 0005509 | molecular_function | calcium ion binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0008047 | molecular_function | enzyme activator activity |
D | 0020007 | cellular_component | apical complex |
D | 0046872 | molecular_function | metal ion binding |
D | 0061891 | molecular_function | calcium ion sensor activity |
F | 0004860 | molecular_function | protein kinase inhibitor activity |
F | 0005576 | cellular_component | extracellular region |
G | 0004860 | molecular_function | protein kinase inhibitor activity |
G | 0005576 | cellular_component | extracellular region |
H | 0004860 | molecular_function | protein kinase inhibitor activity |
H | 0005576 | cellular_component | extracellular region |
I | 0004860 | molecular_function | protein kinase inhibitor activity |
I | 0005576 | cellular_component | extracellular region |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL |
Chain | Residue | Details |
A | ASP20-LEU32 | |
A | ASP56-PHE68 | |
A | ASP93-LEU105 | |
A | ASP129-PHE141 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | SITE: Important for the flexibility at the center of the helix, flexibility that is important for the stability of the voltage-gated pore => ECO:0000269|PubMed:2187536 |
Chain | Residue | Details |
F | PRO14 | |
A | GLU67 | |
A | ASP93 | |
A | ASP95 | |
A | ASP97 | |
A | TYR99 | |
A | GLU104 | |
A | ASP129 | |
A | ASP131 | |
A | ASP133 | |
A | GLN135 | |
G | PRO14 | |
A | GLU140 | |
B | ASP20 | |
B | ASP22 | |
B | ASP24 | |
B | THR26 | |
B | GLU31 | |
B | ASP56 | |
B | ASP58 | |
B | ASN60 | |
B | THR62 | |
H | PRO14 | |
B | GLU67 | |
B | ASP93 | |
B | ASP95 | |
B | ASP97 | |
B | TYR99 | |
B | GLU104 | |
B | ASP129 | |
B | ASP131 | |
B | ASP133 | |
B | GLN135 | |
I | PRO14 | |
B | GLU140 | |
C | ASP20 | |
C | ASP22 | |
C | ASP24 | |
C | THR26 | |
C | GLU31 | |
C | ASP56 | |
C | ASP58 | |
C | ASN60 | |
C | THR62 | |
A | GLU31 | |
C | GLU67 | |
C | ASP93 | |
C | ASP95 | |
C | ASP97 | |
C | TYR99 | |
C | GLU104 | |
C | ASP129 | |
C | ASP131 | |
C | ASP133 | |
C | GLN135 | |
A | ASP56 | |
C | GLU140 | |
D | ASP20 | |
D | ASP22 | |
D | ASP24 | |
D | THR26 | |
D | GLU31 | |
D | ASP56 | |
D | ASP58 | |
D | ASN60 | |
D | THR62 | |
A | ASP58 | |
D | GLU67 | |
D | ASP93 | |
D | ASP95 | |
D | ASP97 | |
D | TYR99 | |
D | GLU104 | |
D | ASP129 | |
D | ASP131 | |
D | ASP133 | |
D | GLN135 | |
A | ASN60 | |
D | GLU140 | |
A | THR62 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: N-formylglycine; partial => ECO:0000269|PubMed:5139483 |
Chain | Residue | Details |
F | GLY1 | |
G | GLY1 | |
H | GLY1 | |
I | GLY1 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Glutamine amide => ECO:0000269|PubMed:5592400 |
Chain | Residue | Details |
F | GLN26 | |
G | GLN26 | |
H | GLN26 | |
I | GLN26 |