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 PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NA A 301 |
Chain | Residue |
A | SER10 |
A | PRO11 |
A | TYR13 |
A | GLN15 |
A | TYR17 |
A | THR106 |
A | GLY107 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 302 |
Chain | Residue |
A | ASP98 |
A | SER100 |
A | ASN101 |
A | GLU45 |
A | ASP53 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 303 |
Chain | Residue |
A | ASP116 |
A | ILE117 |
A | GLU119 |
A | ASN134 |
A | PHE135 |
A | GLY138 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 304 |
Chain | Residue |
A | GLU211 |
A | ASP221 |
A | ASP260 |
A | THR262 |
A | GLY263 |
A | GLN264 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 301 |
Chain | Residue |
B | SER174 |
B | PRO175 |
B | LYS179 |
B | TYR181 |
B | LYS266 |
B | GLY267 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 302 |
Chain | Residue |
B | GLU45 |
B | ASP53 |
B | ASP98 |
B | SER100 |
B | ASN101 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 303 |
Chain | Residue |
B | ASP116 |
B | ILE117 |
B | GLU119 |
B | ASN134 |
B | PHE135 |
B | GLY138 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 304 |
Chain | Residue |
B | GLU211 |
B | ASP221 |
B | ASP260 |
B | THR262 |
B | GLY263 |
B | GLN264 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA C 301 |
Chain | Residue |
C | SER174 |
C | PRO175 |
C | TYR177 |
C | LYS179 |
C | TYR181 |
C | LYS266 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA C 302 |
Chain | Residue |
C | ASP53 |
C | ASP98 |
C | SER100 |
C | ASN101 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 303 |
Chain | Residue |
C | ASP116 |
C | ILE117 |
C | GLU119 |
C | ASN134 |
C | PHE135 |
C | GLY138 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 304 |
Chain | Residue |
C | GLU211 |
C | ASP221 |
C | ASP260 |
C | THR262 |
C | GLY263 |
C | GLN264 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NA D 301 |
Chain | Residue |
D | SER10 |
D | PRO11 |
D | ASN12 |
D | TYR13 |
D | GLN15 |
D | TYR17 |
D | THR106 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA D 302 |
Chain | Residue |
D | GLU45 |
D | ASP53 |
D | ASP98 |
D | SER100 |
D | ASN101 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 303 |
Chain | Residue |
D | ASP116 |
D | ILE117 |
D | GLU119 |
D | ASN134 |
D | PHE135 |
D | GLY138 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 304 |
Chain | Residue |
D | GLU211 |
D | ASP221 |
D | ASP260 |
D | THR262 |
D | GLY263 |
D | GLN264 |
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CnNfiggYfCsC |
Chain | Residue | Details |
A | CYS132-CYS143 | |
site_id | PS01187 |
Number of Residues | 26 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DiNECtdfvdvp.......Cshf....CnNfiggYfC |
Chain | Residue | Details |
A | ASP116-CYS141 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 36 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU45 | |
B | GLU45 | |
B | ASP53 | |
B | ASP98 | |
B | ASP116 | |
B | ILE117 | |
B | GLU119 | |
B | ASN134 | |
B | PHE135 | |
B | GLY138 | |
C | GLU45 | |
A | ASP53 | |
C | ASP53 | |
C | ASP98 | |
C | ASP116 | |
C | ILE117 | |
C | GLU119 | |
C | ASN134 | |
C | PHE135 | |
C | GLY138 | |
D | GLU45 | |
D | ASP53 | |
A | ASP98 | |
D | ASP98 | |
D | ASP116 | |
D | ILE117 | |
D | GLU119 | |
D | ASN134 | |
D | PHE135 | |
D | GLY138 | |
A | ASP116 | |
A | ILE117 | |
A | GLU119 | |
A | ASN134 | |
A | PHE135 | |
A | GLY138 | |
Chain | Residue | Details |
A | ASN134 | |
B | ASN134 | |
C | ASN134 | |
D | ASN134 | |
Chain | Residue | Details |
A | ASN159 | |
B | ASN159 | |
C | ASN159 | |
D | ASN159 | |