Functional Information from GO Data
| Chain | GOid | namespace | contents |
| H | 0002250 | biological_process | adaptive immune response |
| H | 0002376 | biological_process | immune system process |
| H | 0003823 | molecular_function | antigen binding |
| H | 0005576 | cellular_component | extracellular region |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0006955 | biological_process | immune response |
| H | 0019814 | cellular_component | immunoglobulin complex |
| L | 0002250 | biological_process | adaptive immune response |
| L | 0002376 | biological_process | immune system process |
| L | 0003823 | molecular_function | antigen binding |
| L | 0005576 | cellular_component | extracellular region |
| L | 0005886 | cellular_component | plasma membrane |
| L | 0006955 | biological_process | immune response |
| L | 0019814 | cellular_component | immunoglobulin complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PME H 217 |
| Chain | Residue |
| H | TYR34 |
| L | PME217 |
| H | SER36 |
| H | TYR38 |
| H | SER91 |
| H | TYR93 |
| H | PHE101 |
| L | TYR34 |
| L | TYR38 |
| L | PHE99 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PME L 217 |
| Chain | Residue |
| H | TYR34 |
| H | TYR51 |
| H | GLU52 |
| H | PME217 |
| L | TYR32 |
| L | TYR34 |
| L | TYR93 |
| L | ASP97 |
| L | PHE99 |
| L | PRO145 |
| L | GLU202 |
Functional Information from PROSITE/UniProt
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCQVTH |
| Chain | Residue | Details |
| L | TYR195-HIS201 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Region: {"description":"Complementarity-determining-1","evidences":[{"source":"UniProtKB","id":"P01721","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Region: {"description":"Framework-2","evidences":[{"source":"UniProtKB","id":"P01721","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Region: {"description":"Complementarity-determining-2","evidences":[{"source":"UniProtKB","id":"P01721","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 70 |
| Details | Region: {"description":"Framework-3","evidences":[{"source":"UniProtKB","id":"P01721","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 42 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | Region: {"description":"Complementarity-determining-3","evidences":[{"source":"UniProtKB","id":"P01721","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
