5O32
The structure of complement complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004866 | molecular_function | endopeptidase inhibitor activity |
B | 0004866 | molecular_function | endopeptidase inhibitor activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
D | 0016020 | cellular_component | membrane |
E | 0004866 | molecular_function | endopeptidase inhibitor activity |
F | 0004866 | molecular_function | endopeptidase inhibitor activity |
F | 0005576 | cellular_component | extracellular region |
F | 0005615 | cellular_component | extracellular space |
H | 0016020 | cellular_component | membrane |
I | 0004252 | molecular_function | serine-type endopeptidase activity |
I | 0006508 | biological_process | proteolysis |
J | 0004252 | molecular_function | serine-type endopeptidase activity |
J | 0006508 | biological_process | proteolysis |
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 |
I | LEU376-CYS381 |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAckGDSGGPLV |
Chain | Residue | Details |
I | ASP519-VAL530 |
site_id | PS00477 |
Number of Residues | 9 |
Details | ALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEQnM |
Chain | Residue | Details |
B | PRO1007-MET1015 |
site_id | PS01209 |
Number of Residues | 23 |
Details | LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIpsqyq.CNgevDCitg.EDEvg...C |
Chain | Residue | Details |
D | CYS271-CYS293 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Charge relay system => ECO:0000250|UniProtKB:P00750 |
Chain | Residue | Details |
I | HIS380 | |
D | ASP283 | |
D | ASP289 | |
D | GLU290 | |
H | LYS239 | |
H | ASP242 | |
H | ILE244 | |
H | ASP246 | |
H | ASP252 | |
H | GLU253 | |
H | TYR276 | |
I | ASP429 | |
H | ASN279 | |
H | GLU281 | |
H | ASP283 | |
H | ASP289 | |
H | GLU290 | |
I | SER525 | |
J | HIS380 | |
J | ASP429 | |
J | SER525 | |
D | TYR276 | |
D | ASN279 | |
D | GLU281 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC |
Chain | Residue | Details |
I | ASN464 | |
J | ASN464 | |
H | ASN70 | |
H | ASN177 | |
E | SER38 | |
E | SER70 | |
E | SER297 | |
E | SER303 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC |
Chain | Residue | Details |
I | ASN494 | |
J | ASN494 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC |
Chain | Residue | Details |
I | ASN536 | |
J | ASN536 | |
B | SER1573 | |
F | SER968 | |
F | SER1321 | |
F | SER1573 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17051150 |
Chain | Residue | Details |
B | ASN939 | |
F | ASN939 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 |
Chain | Residue | Details |
B | ASN1617 | |
F | ASN1617 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | CROSSLNK: Isoglutamyl cysteine thioester (Cys-Gln) |
Chain | Residue | Details |
B | CYS1010 | |
B | GLN1013 | |
F | CYS1010 | |
F | GLN1013 |