Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| B | 0005576 | cellular_component | extracellular region |
| C | 0005576 | cellular_component | extracellular region |
| D | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 1001 |
| Chain | Residue |
| B | SER441 |
| B | GLU447 |
| B | GLU522 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 1002 |
| Chain | Residue |
| D | SER641 |
| D | GLN643 |
| D | GLU647 |
| D | GLU722 |
Functional Information from PROSITE/UniProt
| site_id | PS00615 |
| Number of Residues | 26 |
| Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CFalekdlgfvl..WINLYCaqknp.FVC |
| Chain | Residue | Details |
| A | CYS103-CYS128 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 240 |
| Details | Domain: {"description":"C-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]} |
1FVU
