Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
D | 0005509 | molecular_function | calcium ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 300 |
Chain | Residue |
A | GLU48 |
A | ASP56 |
A | ASP101 |
A | SER103 |
A | ASN104 |
A | HOH419 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue CA A 301 |
Chain | Residue |
A | ASN139 |
A | TYR140 |
A | GLY143 |
A | HOH408 |
A | ASP119 |
A | VAL120 |
A | GLU122 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA A 302 |
Chain | Residue |
A | GLU215 |
A | ASP225 |
A | ASP262 |
A | SER264 |
A | HOH417 |
A | HOH420 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA D 300 |
Chain | Residue |
D | GLU48 |
D | ASP56 |
D | ASP101 |
D | SER103 |
D | ASN104 |
D | HOH415 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue CA D 301 |
Chain | Residue |
D | ASP119 |
D | VAL120 |
D | GLU122 |
D | ASN139 |
D | TYR140 |
D | GLY143 |
D | HOH411 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue CA D 302 |
Chain | Residue |
D | GLU215 |
D | ASP225 |
D | ASP262 |
D | SER264 |
D | HOH413 |
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ChNylggYyCsC |
Chain | Residue | Details |
A | CYS137-CYS148 | |
site_id | PS01186 |
Number of Residues | 16 |
Details | EGF_2 EGF-like domain signature 2. CsCrvGYilhqnkhtC |
Chain | Residue | Details |
A | CYS146-CYS161 | |
site_id | PS01187 |
Number of Residues | 28 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DvDECrtslgdsvp.....Cdhy....ChNylggYyC |
Chain | Residue | Details |
A | ASP119-CYS146 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLU48 | |
D | SER103 | |
D | ASN104 | |
D | GLY143 | |
A | ASP56 | |
A | ASP101 | |
A | SER103 | |
A | ASN104 | |
A | GLY143 | |
D | GLU48 | |
D | ASP56 | |
D | ASP101 | |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP119 | |
A | VAL120 | |
A | TYR140 | |
D | ASP119 | |
D | VAL120 | |
D | TYR140 | |
Chain | Residue | Details |
A | ASN139 | |
D | ASN139 | |
Chain | Residue | Details |
A | ASN84 | |
D | ASN84 | |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN266 | |
D | ASN266 | |