Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue HEZ A 501 |
| Chain | Residue |
| A | GLY109 |
| A | SER110 |
| A | MET111 |
| A | SER120 |
| A | THR121 |
| A | SER156 |
| A | HOH613 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | GLU202 |
| A | ASN214 |
| A | ASP215 |
| A | HOH601 |
| A | HOH608 |
| A | GLU195 |
| A | ASN197 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 503 |
| Chain | Residue |
| A | ASP171 |
| A | GLU175 |
| A | GLN199 |
| A | GLU202 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| A | GLY217 |
| A | LEU219 |
| A | GLN220 |
| A | HOH662 |
| A | HOH683 |
Functional Information from PROSITE/UniProt
| site_id | PS00615 |
| Number of Residues | 23 |
| Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CVemytdgt.....WNDRGClqyrl.AVC |
| Chain | Residue | Details |
| A | CYS204-CYS226 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 115 |
| Details | Domain: {"description":"C-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]} |
