Functional Information from GO Data
Chain | GOid | namespace | contents |
L | 0002250 | biological_process | adaptive immune response |
L | 0002376 | biological_process | immune system process |
L | 0003094 | biological_process | glomerular filtration |
L | 0003823 | molecular_function | antigen binding |
L | 0005576 | cellular_component | extracellular region |
L | 0005615 | cellular_component | extracellular space |
L | 0005886 | cellular_component | plasma membrane |
L | 0006955 | biological_process | immune response |
L | 0016020 | cellular_component | membrane |
L | 0019731 | biological_process | antibacterial humoral response |
L | 0019814 | cellular_component | immunoglobulin complex |
L | 0070062 | cellular_component | extracellular exosome |
L | 0071748 | cellular_component | monomeric IgA immunoglobulin complex |
L | 0071751 | cellular_component | secretory IgA immunoglobulin complex |
L | 0071756 | cellular_component | pentameric IgM immunoglobulin complex |
L | 0072562 | cellular_component | blood microparticle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL L 201 |
Chain | Residue |
L | GLN37 |
L | GLN38 |
L | LYS39 |
L | GLN42 |
L | ALA43 |
L | ARG45 |
L | HOH357 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL L 202 |
Chain | Residue |
L | SER63 |
L | GLY64 |
L | SER67 |
L | GLY68 |
L | THR69 |
L | ASP70 |
L | HOH323 |
L | SER52 |
L | ARG54 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL L 203 |
Chain | Residue |
H | GLY15 |
H | GLY42 |
L | GLY9 |
L | GLN100 |
L | GLY101 |
L | HOH383 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE TMO L 204 |
Chain | Residue |
H | THR97 |
H | GLN101 |
L | TYR49 |
L | ALA55 |
L | THR56 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 95 |
Details | Domain: {"description":"Ig-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 22 |
Details | Region: {"description":"Framework-1","evidences":[{"source":"UniProtKB","id":"P01602","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 11 |
Details | Region: {"description":"Complementarity-determining-1","evidences":[{"source":"UniProtKB","id":"P01602","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | Region: {"description":"Framework-2","evidences":[{"source":"UniProtKB","id":"P01602","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | Region: {"description":"Complementarity-determining-2","evidences":[{"source":"UniProtKB","id":"P01602","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 31 |
Details | Region: {"description":"Framework-3","evidences":[{"source":"UniProtKB","id":"P01602","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | Region: {"description":"Complementarity-determining-3","evidences":[{"source":"UniProtKB","id":"P01602","evidenceCode":"ECO:0000250"}]} |