2OAY
Crystal structure of latent human C1-inhibitor
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00284 |
Number of Residues | 11 |
Details | SERPIN Serpins signature. FEVQQPFLFmL |
Chain | Residue | Details |
A | PHE449-LEU459 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Reactive bond for chymotrypsin |
Chain | Residue | Details |
A | ALA443 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Reactive bond |
Chain | Residue | Details |
A | ARG444 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17488724, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3756141 |
Chain | Residue | Details |
A | ASN216 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3756141 |
Chain | Residue | Details |
A | ASN231 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; in variant TA |
Chain | Residue | Details |
A | ASN250 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:3756141 |
Chain | Residue | Details |
A | ASN330 |