Crystal structure of human coagulation factor IXa (S195A), apo-form, DES-GLA. Determined by X-ray diffraction at 1.88 Å resolution. Released 3 Jul 2024.
Explore 8EPH in 3D Show helices and sheets RCSB PDB PDBe
8EPH contains 30 α-helices and 60 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 50-53 | 4 | |
| α-helix | 60 | 1 | |
| β-strand | 61-65 | 5 | 1 |
| β-strand | 68-72 | 5 | 1 |
| α-helix | 73-74 | 2 | |
| β-strand | 77-78 | 2 | 2 |
| β-strand | 84-85 | 2 | 2 |
| α-helix | 86 | 1 | |
| α-helix | 91-94 | 4 | |
| β-strand | 98-101 | 4 | 3 |
| α-helix | 102 | 1 | |
| β-strand | 107-110 | 4 | 3 |
| β-strand | 115-117 | 3 | 4 |
| β-strand | 124-126 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 5 |
| β-strand | 20-21 | 2 | 6 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 7 |
| β-strand | 42-48 | 7 | 7 |
| β-strand | 51-54 | 4 | 7 |
| α-helix | 56-58 | 3 | |
| β-strand | 65-68 | 4 | 7 |
| β-strand | 72 | 1 | 8 |
| β-strand | 81-90 | 10 | 7 |
| β-strand | 104-108 | 5 | 7 |
| β-strand | 115 | 1 | 9 |
| β-strand | 118 | 1 | 9 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 6 |
| α-helix | 126-132 | 9 | |
| β-strand | 135-140 | 6 | 6 |
| β-strand | 143 | 1 | 10 |
| α-helix | 150 | 1 | |
| β-strand | 151 | 1 | 10 |
| α-helix | 152 | 1 | |
| β-strand | 154 | 1 | 8 |
| β-strand | 156-163 | 8 | 6 |
| α-helix | 165-170 | 6 | |
| β-strand | 180-183 | 4 | 6 |
| β-strand | 189 | 1 | 5 |
| β-strand | 198-203 | 6 | 6 |
| β-strand | 206-216 | 11 | 6 |
| β-strand | 226-230 | 5 | 6 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-242 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 50-53 | 4 | |
| α-helix | 60 | 1 | |
| β-strand | 61-65 | 5 | 11 |
| β-strand | 68-72 | 5 | 11 |
| α-helix | 73-74 | 2 | |
| β-strand | 77-78 | 2 | 12 |
| β-strand | 84-85 | 2 | 12 |
| α-helix | 86 | 1 | |
| α-helix | 91-94 | 4 | |
| β-strand | 98-101 | 4 | 13 |
| α-helix | 103-105 | 3 | |
| β-strand | 107-110 | 4 | 13 |
| β-strand | 115-117 | 3 | 14 |
| β-strand | 124-126 | 3 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Coagulation factor IXa light chain | A, C | protein | 102 | Homo sapiens | P00740 (AlphaFold model) |
| Coagulation factor IXa heavy chain | B, D | protein | 235 | Homo sapiens | P00740 (AlphaFold model) |
>8EPH_1 Coagulation factor IXa light chain (chains A, C) DGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNK VVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRRKR
>8EPH_2 Coagulation factor IXa heavy chain (chains B, D) VVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEE TEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFL KFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDS CQGDAGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
An RNA aptamer exploits exosite-dependent allostery to achieve specific inhibition of coagulation factor IXa. Kolyadko, V.N., Layzer, J.M., Perry, K. et al. Proc Natl Acad Sci U S A (2024) 121:e2401136121-e2401136121. DOI 10.1073/pnas.2401136121 · PubMed
Other PDB entries of the same protein (UniProt P00740 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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