9CTH
Preliminary map of the Prothrombin-prothrombinase complex on nano discs
This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDglgeYtCtC |
Chain | Residue | Details |
B | CYS61-CYS72 |
site_id | PS00011 |
Number of Residues | 26 |
Details | GLA_1 Vitamin K-dependent carboxylation domain. EcmEEtCsyeearEvfedsdktne.FW |
Chain | Residue | Details |
B | GLU16-TRP41 | |
D | GLU16-TRP41 |
site_id | PS00021 |
Number of Residues | 14 |
Details | KRINGLE_1 Kringle domain signature. FCRNpdssttgpWC |
Chain | Residue | Details |
D | PHE113-CYS126 | |
D | PHE218-CYS231 |
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CtCleGfeGKnC |
Chain | Residue | Details |
B | CYS70-CYS81 |
site_id | PS00079 |
Number of Residues | 21 |
Details | MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GkWiIsSlTPkhLqAGMqayI |
Chain | Residue | Details |
A | GLY276-ILE296 | |
E | GLY1852-PHE1872 |
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
Chain | Residue | Details |
C | LEU53-CYS58 | |
D | LEU359-CYS364 |
site_id | PS01186 |
Number of Residues | 12 |
Details | EGF_2 EGF-like domain signature 2. CtCleGFegkn....C |
Chain | Residue | Details |
B | CYS70-CYS81 | |
B | CYS109-CYS124 |
site_id | PS01187 |
Number of Residues | 25 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC |
Chain | Residue | Details |
B | ASP46-CYS70 |
site_id | PS01285 |
Number of Residues | 34 |
Details | FA58C_1 Coagulation factors 5/8 type C domain (FA58C) signature 1. AWsveklaaefaskp..WIqVDmqkeviItgIqTQG |
Chain | Residue | Details |
E | ALA1919-GLY1952 | |
E | ALA2083-GLY2112 |
site_id | PS01286 |
Number of Residues | 17 |
Details | FA58C_2 Coagulation factors 5/8 type C domain (FA58C) signature 2. Ptraynrpt..LRlELqGC |
Chain | Residue | Details |
E | PRO2017-CYS2033 | |
E | PRO2177-CYS2193 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Charge relay system |
Chain | Residue | Details |
D | HIS363 | |
B | GLU32 | |
B | GLU39 | |
D | ASP419 | |
D | ALA525 | |
B | GLU16 | |
B | GLU19 | |
B | GLU20 | |
B | GLU25 | |
B | GLU26 | |
B | GLU29 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Cleavage; by thrombin |
Chain | Residue | Details |
D | ARG155 | |
A | ARG506 | |
A | ARG679 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Cleavage; by factor Xa => ECO:0000269|PubMed:34265300 |
Chain | Residue | Details |
D | ARG271 | |
D | ARG320 | |
E | ASN2181 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407 |
Chain | Residue | Details |
D | GLU6 | |
D | GLU7 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:6305407 |
Chain | Residue | Details |
D | GLU14 | |
D | GLU16 | |
D | GLU19 | |
D | GLU20 | |
D | GLU25 | |
D | GLU26 | |
D | GLU29 | |
D | GLU32 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320 |
Chain | Residue | Details |
D | ASN78 | |
D | ASN100 | |
A | ASN211 | |
A | ASN354 | |
A | ASN440 | |
A | ASN526 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923 |
Chain | Residue | Details |
D | ASN373 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 |
Chain | Residue | Details |
A | ASN432 |