Crystal structure of prethrombin-2 with a peptide corresponding to the C-terminus of the heavy chain of factor Va. Determined by X-ray diffraction at 2.8 Å resolution. Released 12 Aug 2026.
Explore 9T00 in 3D Show helices and sheets RCSB PDB PDBe
9T00 contains 35 α-helices and 42 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 | 283-286 | 4 | |
| α-helix | 290-292 | 3 | |
| α-helix | 300-302 | 3 | |
| α-helix | 309-311 | 3 | |
| α-helix | 313-315 | 3 | |
| β-strand | 325-326 | 2 | 1 |
| α-helix | 327-328 | 2 | |
| β-strand | 335-340 | 6 | 2 |
| β-strand | 346-352 | 7 | 2 |
| β-strand | 357-360 | 4 | 2 |
| α-helix | 362-365 | 4 | |
| β-strand | 366-367 | 2 | 3 |
| α-helix | 368-370 | 3 | |
| β-strand | 372-373 | 2 | 3 |
| α-helix | 376-378 | 3 | |
| β-strand | 379-383 | 5 | 2 |
| β-strand | 387 | 1 | 4 |
| β-strand | 397-399 | 3 | 2 |
| β-strand | 401-406 | 6 | 2 |
| β-strand | 411 | 1 | 5 |
| β-strand | 417 | 1 | 5 |
| β-strand | 421-425 | 5 | 2 |
| α-helix | 437-438 | 2 | |
| β-strand | 439 | 1 | 1 |
| α-helix | 443-449 | 7 | |
| β-strand | 455-460 | 6 | 1 |
| α-helix | 463-468 | 6 | |
| β-strand | 479 | 1 | 4 |
| β-strand | 481-487 | 7 | 1 |
| α-helix | 488-489 | 2 | |
| α-helix | 490-495 | 6 | |
| β-strand | 505-508 | 4 | 1 |
| α-helix | 524 | 1 | |
| β-strand | 528-532 | 5 | 1 |
| β-strand | 539-545 | 7 | 1 |
| β-strand | 558-562 | 5 | 1 |
| α-helix | 564-566 | 3 | |
| α-helix | 567-575 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 693-705 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 283-286 | 4 | |
| α-helix | 290-292 | 3 | |
| α-helix | 300-302 | 3 | |
| α-helix | 308-311 | 4 | |
| β-strand | 325-326 | 2 | 6 |
| α-helix | 327-328 | 2 | |
| β-strand | 335-340 | 6 | 7 |
| β-strand | 345-352 | 8 | 7 |
| β-strand | 357-360 | 4 | 7 |
| α-helix | 362-365 | 4 | |
| β-strand | 366-367 | 2 | 8 |
| α-helix | 368-370 | 3 | |
| β-strand | 372-373 | 2 | 8 |
| α-helix | 376-378 | 3 | |
| β-strand | 379-383 | 5 | 7 |
| β-strand | 387 | 1 | 9 |
| β-strand | 397-399 | 3 | 7 |
| β-strand | 401-406 | 6 | 7 |
| β-strand | 411 | 1 | 10 |
| β-strand | 417 | 1 | 10 |
| β-strand | 421-425 | 5 | 7 |
| α-helix | 437-438 | 2 | |
| β-strand | 439 | 1 | 6 |
| α-helix | 443-449 | 7 | |
| β-strand | 455-460 | 6 | 6 |
| α-helix | 463-468 | 6 | |
| β-strand | 479 | 1 | 9 |
| β-strand | 481-487 | 7 | 6 |
| α-helix | 488-489 | 2 | |
| α-helix | 490-495 | 6 | |
| β-strand | 505-508 | 4 | 6 |
| α-helix | 524 | 1 | |
| β-strand | 528-532 | 5 | 6 |
| β-strand | 539-545 | 7 | 6 |
| β-strand | 558-562 | 5 | 6 |
| α-helix | 564-566 | 3 | |
| α-helix | 567-575 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Prothrombin | A, C | protein | 314 | Homo sapiens | P00734 (AlphaFold model) |
| Coagulation factor V heavy chain | B, D | protein | 24 | Homo sapiens | P12259 (AlphaFold model) |
>9T00_1 Prothrombin (chains A, C) MAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGS DAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGK HSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRET AASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNM FCAGYKPDEGKRGDACEGDAGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFR LKKWIQKVIDQFGE
>9T00_2 Coagulation factor V heavy chain (chains B, D) EPEDEESDADYDYQNRLAAALGIR
Prothrombinase processivity is conferred by substrate allostery. Ustok, F.I., Faille, A., Warren, A.J. et al. EMBO J (2026) 45:3954-3977. DOI 10.1038/s44318-026-00782-4 · PubMed
Other PDB entries of the same protein (UniProt P00734 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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