2ODQ
Complement component C2a, the catalytic fragment of C3- and C5-convertase of human complement
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
Chain | Residue | Details |
A | LEU483-CYS488 |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. SPckGESGGAVF |
Chain | Residue | Details |
A | SER653-PHE664 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Motif: {"description":"MIDAS-like motif","evidences":[{"source":"PubMed","id":"17027507","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17027507","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17234210","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ODQ","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | ASP541 | |
A | HIS487 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | SER659 | |
A | GLY660 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | GLY657 | |
A | SER659 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | SER659 | |
A | ASP541 | |
A | HIS487 |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | SER659 | |
A | ASP541 | |
A | HIS487 | |
A | GLY660 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | GLY657 | |
A | SER659 | |
A | ASP541 | |
A | HIS487 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 688 |
Chain | Residue | Details |
A | HIS487 | proton acceptor, proton donor |
A | ASP541 | electrostatic stabiliser |
A | SER659 | electrostatic stabiliser |