Coagulation factor Xa complex with a2-loop peptide. Determined by X-ray diffraction at 1.2 Å resolution. Released 26 Nov 2025.
Explore 9I24 in 3D Show helices and sheets RCSB PDB PDBe
9I24 contains 10 α-helices and 26 β-strands across 3 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 |
|---|---|---|---|
| β-strand | 16-19 | 4 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 3 |
| β-strand | 40-46 | 7 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-60 | 5 | |
| β-strand | 65-68 | 4 | 3 |
| β-strand | 81-83 | 3 | 3 |
| β-strand | 85-91 | 7 | 3 |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 115 | 1 | 4 |
| β-strand | 118 | 1 | 4 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-124A | 3 | |
| α-helix | 125-127 | 3 | |
| α-helix | 128-131A | 5 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 143 | 1 | 5 |
| β-strand | 151 | 1 | 5 |
| β-strand | 156-163 | 8 | 2 |
| α-helix | 165-171 | 7 | |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-203 | 6 | 2 |
| β-strand | 206-215 | 10 | 2 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-241 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 92-95 | 4 | |
| β-strand | 99-103 | 5 | 6 |
| β-strand | 106-110 | 5 | 6 |
| β-strand | 115-117 | 3 | 7 |
| β-strand | 124-126 | 3 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Activated factor Xa heavy chain | H | protein | 254 | Homo sapiens | P00742 (AlphaFold model) |
| Factor X light chain | L | protein | 55 | Homo sapiens | P00742 (AlphaFold model) |
| Coagulation factor V heavy chain | C | protein | 15 | synthetic construct | P12259 (AlphaFold model) |
| GLU-GLY-ARG-chloromethyl ketone inhibitor (EGRCK) | I | protein | 3 | synthetic construct |
>9I24_1 Activated factor Xa heavy chain (chains H) IVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTE QEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLM TQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDA CQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTKTRGLP KAKSHAPEVITSSP
>9I24_2 Factor X light chain (chains L) MRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLER
>9I24_3 Coagulation factor V heavy chain (chains C) CIPDDDEDSYEIFEP
>9I24_4 GLU-GLY-ARG-chloromethyl ketone inhibitor (EGRCK) (chains I) EGR
| ID | Name | Formula | Copies |
|---|---|---|---|
| 0GJ | L-alpha-glutamyl-N-{(1S)-4-{[amino(iminio)methyl]amino}-1-[(1S)-2-chloro-1-hydr… | C14 H28 Cl N6 O5 | 1 |
| CA | Calcium ion | Ca | 1 |
Water and common crystallization additives (IMD, CL, NA) are not listed.
A 3.3- angstrom cryo-EM structure of an engineered high-affinity human prothrombinase complex. Ustok, F.I., Faille, A., Huntington, J.A. Blood (2026) 147:573-583. DOI 10.1182/blood.2025031527 · PubMed
Other PDB entries of the same protein (UniProt P00742 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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