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 | 0016020 | cellular_component | membrane |
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 | 0016020 | cellular_component | membrane |
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"}]} |