Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
B | 0005509 | molecular_function | calcium ion binding |
C | 0005509 | molecular_function | calcium ion binding |
D | 0005509 | molecular_function | calcium ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ChNyvggYfCsC |
Chain | Residue | Details |
A | CYS148-CYS159 | |
D | CYS132-CYS143 | |
site_id | PS01186 |
Number of Residues | 16 |
Details | EGF_2 EGF-like domain signature 2. CsCrpGYelqedthsC |
Chain | Residue | Details |
A | CYS157-CYS172 | |
site_id | PS01187 |
Number of Residues | 33 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DlDECasrsksgeedpqpqCqhl....ChNyvggYfC |
Chain | Residue | Details |
A | ASP125-CYS157 | |
D | ASP116-CYS141 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
Details | BINDING: |
Chain | Residue | Details |
D | GLU45 | |
B | GLU45 | |
B | ASP53 | |
B | ASP98 | |
B | ASP116 | |
B | ILE117 | |
B | GLU119 | |
B | ASN134 | |
B | PHE135 | |
B | GLY138 | |
D | ASP53 | |
D | ASP98 | |
D | ASP116 | |
D | ILE117 | |
D | GLU119 | |
D | ASN134 | |
D | PHE135 | |
D | GLY138 | |
Chain | Residue | Details |
D | ASN134 | |
B | ASN134 | |
Chain | Residue | Details |
D | ASN159 | |
B | ASN159 | |
C | ASN108 | |
C | ASN204 | |