Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0090729 | molecular_function | toxin activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0090729 | molecular_function | toxin activity |
| G | 0005509 | molecular_function | calcium ion binding |
| G | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 501 |
| Chain | Residue |
| A | SER41 |
| A | GLU43 |
| A | GLU47 |
| A | GLU128 |
| A | HOH568 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 502 |
| Chain | Residue |
| B | HOH529 |
| B | HOH554 |
| B | SER241 |
| B | GLN243 |
| B | GLU247 |
| B | GLU320 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA G 503 |
| Chain | Residue |
| A | GLU98 |
| B | HOH505 |
| G | CGU425 |
| G | CGU429 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA G 504 |
| Chain | Residue |
| G | HOH47 |
| G | HOH62 |
| G | CGU407 |
| G | CGU426 |
| G | CGU429 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CA G 505 |
| Chain | Residue |
| G | HOH63 |
| G | HOH102 |
| G | HOH125 |
| G | CGU407 |
| G | CGU416 |
| G | CGU426 |
| G | CGU429 |
| G | CA506 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA G 506 |
| Chain | Residue |
| G | ALA401 |
| G | ASN402 |
| G | CGU406 |
| G | CGU407 |
| G | CGU416 |
| G | CGU426 |
| G | CA505 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA G 507 |
| Chain | Residue |
| G | HOH123 |
| G | ALA401 |
| G | CGU406 |
| G | CGU416 |
| G | CGU420 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA G 508 |
| Chain | Residue |
| G | HOH37 |
| G | HOH143 |
| G | HOH149 |
| G | HOH190 |
| G | CGU420 |
| G | CGU420 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA G 509 |
| Chain | Residue |
| G | HOH204 |
| G | HOH218 |
| G | CGU414 |
| G | CGU419 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA G 510 |
| Chain | Residue |
| G | CGU435 |
| G | CGU439 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 511 |
| Chain | Residue |
| A | SER80 |
| A | SER80 |
| A | GLU82 |
| A | GLU82 |
| A | HOH580 |
| A | HOH580 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 512 |
| Chain | Residue |
| A | ASP1 |
| A | ASP1 |
| A | HOH575 |
| A | HOH575 |
Functional Information from PROSITE/UniProt
| site_id | PS00011 |
| Number of Residues | 26 |
| Details | GLA_1 Vitamin K-dependent carboxylation domain. EclEEaCsleearEvfedaeqtde.FW |
| Chain | Residue | Details |
| G | CGU416-TRP441 | |
| site_id | PS00615 |
| Number of Residues | 26 |
| Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CLgvhietgfhk..WENFYCeqqdp.FVC |
| Chain | Residue | Details |
| A | CYS102-CYS127 | |
| B | CYS296-CYS319 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 250 |
| Details | Domain: {"description":"C-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {} |