8EPH
Crystal structure of human coagulation factor IXa (S195A), apo-form, DES-GLA
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDdinsYeCwC |
| Chain | Residue | Details |
| A | CYS62-CYS73 |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CwCpfGfeGKnC |
| Chain | Residue | Details |
| A | CYS71-CYS82 |
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC |
| Chain | Residue | Details |
| B | VAL53-CYS58 |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CwCpfGFegkn....C |
| Chain | Residue | Details |
| A | CYS71-CYS82 | |
| A | CYS109-CYS124 |
| site_id | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCesnp..........Clnggs..CkDdinsYeC |
| Chain | Residue | Details |
| A | ASP47-CYS71 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:659613 |
| Chain | Residue | Details |
| B | HIS57 | |
| C | ASP65 | |
| B | ALA195 | |
| D | HIS57 | |
| D | ALA195 | |
| A | ASP65 | |
| C | ASP47 | |
| C | GLY48 | |
| C | GLN50 | |
| C | ASP64 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:659613 |
| Chain | Residue | Details |
| B | ASP102 | |
| D | ASP102 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5 |
| Chain | Residue | Details |
| B | GLU70 | |
| B | ASN72 | |
| B | GLU75 | |
| B | GLU77 | |
| D | GLU70 | |
| D | ASN72 | |
| D | GLU75 | |
| D | GLU77 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5 |
| Chain | Residue | Details |
| B | GLU80 | |
| D | GLU80 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (Fuc...) serine => ECO:0000269|PubMed:1517205, ECO:0000269|PubMed:25456591 |
| Chain | Residue | Details |
| A | SER61 | |
| C | SER61 |
