1ZVO
Semi-extended solution structure of human myeloma immunoglobulin D determined by constrained X-ray scattering
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002250 | biological_process | adaptive immune response |
| A | 0002376 | biological_process | immune system process |
| A | 0003823 | molecular_function | antigen binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0016064 | biological_process | immunoglobulin mediated immune response |
| A | 0019814 | cellular_component | immunoglobulin complex |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071735 | cellular_component | IgG immunoglobulin complex |
| A | 0072562 | cellular_component | blood microparticle |
| B | 0002250 | biological_process | adaptive immune response |
| B | 0002376 | biological_process | immune system process |
| B | 0003823 | molecular_function | antigen binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0016064 | biological_process | immunoglobulin mediated immune response |
| B | 0019814 | cellular_component | immunoglobulin complex |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0071735 | cellular_component | IgG immunoglobulin complex |
| B | 0072562 | cellular_component | blood microparticle |
Functional Information from PROSITE/UniProt
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YKCVVQH |
| Chain | Residue | Details |
| C | TYR211-HIS217 | |
| C | TYR482-HIS488 | |
| A | TYR193-HIS199 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 188 |
| Details | Domain: {"description":"Ig-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 184 |
| Details | Domain: {"description":"Ig-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 176 |
| Details | Domain: {"description":"Ig-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 212 |
| Details | Domain: {"description":"Ig-like 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 142 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 24 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 40 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (GalNAc...) serine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1982","firstPage":"463","lastPage":"470","publisher":"Humana Press","address":"Clifton.","bookName":"Methods in protein sequence analysis","title":"Separation of hinge glycopeptides of human IgD by HPLC.","editors":["Elzinga M."],"authors":["Takahashi N.","Tetaert D.","Putnam F.W."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (GalNAc...) serine","evidences":[{"source":"PubMed","id":"7092891","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"source":"PubMed","id":"7092891","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1982","firstPage":"463","lastPage":"470","publisher":"Humana Press","address":"Clifton.","bookName":"Methods in protein sequence analysis","title":"Separation of hinge glycopeptides of human IgD by HPLC.","editors":["Elzinga M."],"authors":["Takahashi N.","Tetaert D.","Putnam F.W."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"6806818","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 192 |
| Details | Domain: {"description":"Ig-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 256 |
| Details | Region: {"description":"Variable (V) domain, involved in antigen recognition","evidences":[{"source":"PubMed","id":"6806818","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 764 |
| Details | Region: {"description":"Constant (C) domain","evidences":[{"source":"PubMed","id":"6806818","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
