4IBL
Rubidium Sites in Blood Coagulation Factor VIIa
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC |
Chain | Residue | Details |
L | CYS61-CYS72 |
site_id | PS00011 |
Number of Residues | 26 |
Details | GLA_1 Vitamin K-dependent carboxylation domain. EckEEqCsfeearEifkdaertkl.FW |
Chain | Residue | Details |
L | CGU16-TRP41 |
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CfClpAfeGRnC |
Chain | Residue | Details |
L | CYS70-CYS81 |
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC |
Chain | Residue | Details |
H | VAL53-CYS58 |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA |
Chain | Residue | Details |
H | ASP189-ALA200 |
site_id | PS00621 |
Number of Residues | 18 |
Details | TISSUE_FACTOR Tissue factor signature. WKsKCfyTtDTECDLTDE |
Chain | Residue | Details |
T | TRP45-GLU62 |
site_id | PS01186 |
Number of Residues | 16 |
Details | EGF_2 EGF-like domain signature 2. CrCheGYslladgvsC |
Chain | Residue | Details |
L | CYS112-CYS127 |
site_id | PS01187 |
Number of Residues | 25 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCassp..........Cqnggs..CkDqlqsYiC |
Chain | Residue | Details |
L | ASP46-CYS70 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 218 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
T | SER1-GLU219 | |
H | ASP102 | |
H | SER195 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
T | ASN124 | |
T | ASN137 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725 |
Chain | Residue | Details |
H | ASN175 | |
L | CGU7 | |
L | CGU14 | |
L | CGU16 | |
L | CGU20 | |
L | CGU25 | |
L | CGU26 | |
L | CGU29 | |
L | CGU35 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725 |
Chain | Residue | Details |
L | CGU19 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:3264725 |
Chain | Residue | Details |
L | ASP63 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (Xyl...) serine; alternate => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:2511201 |
Chain | Residue | Details |
L | SER52 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (Fuc) serine => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:9023546 |
Chain | Residue | Details |
L | SER60 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725 |
Chain | Residue | Details |
L | ASN145 |