Crystal Structure of Blood Coagulation Factor Xa in Complex with Ecotin M84R. Determined by X-ray diffraction at 2.8 Å resolution. Released 26 Aug 2003.
Explore 1P0S in 3D Show helices and sheets RCSB PDB PDBe
1P0S contains 19 α-helices and 38 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 |
|---|---|---|---|
| α-helix | 7-9 | 3 | |
| α-helix | 13-17 | 5 | |
| β-strand | 20-25 | 6 | 9 |
| α-helix | 27-29 | 3 | |
| α-helix | 33-35 | 3 | |
| β-strand | 36-48 | 13 | 10 |
| β-strand | 53 | 1 | 4 |
| β-strand | 55 | 1 | 11 |
| β-strand | 56-64 | 9 | 9 |
| β-strand | 69-78 | 10 | 9 |
| β-strand | 82-83 | 2 | 4 |
| β-strand | 93-98 | 6 | 10 |
| β-strand | 99 | 1 | 11 |
| β-strand | 106-108 | 3 | 10 |
| β-strand | 115-120 | 6 | 9 |
| β-strand | 124-131 | 8 | 10 |
| α-helix | 139-141 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 3 |
| β-strand | 20-21 | 2 | 4 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-35 | 6 | 5 |
| β-strand | 40-46 | 7 | 5 |
| β-strand | 51-54 | 4 | 5 |
| α-helix | 56-59 | 4 | |
| β-strand | 64-68 | 5 | 5 |
| β-strand | 72 | 1 | 6 |
| β-strand | 81-90 | 10 | 5 |
| β-strand | 104-108 | 5 | 5 |
| β-strand | 115 | 1 | 7 |
| β-strand | 118 | 1 | 7 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 4 |
| α-helix | 123-124A | 3 | |
| α-helix | 125-127 | 3 | |
| α-helix | 128-131A | 5 | |
| β-strand | 135-140 | 6 | 4 |
| β-strand | 143 | 1 | 8 |
| β-strand | 151 | 1 | 8 |
| β-strand | 154 | 1 | 6 |
| β-strand | 156-163 | 8 | 4 |
| α-helix | 165-171 | 7 | |
| β-strand | 180-183 | 4 | 4 |
| β-strand | 189 | 1 | 3 |
| β-strand | 198-203 | 6 | 4 |
| β-strand | 206-216 | 11 | 4 |
| β-strand | 226-230 | 5 | 4 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-241 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-13 | 7 | |
| α-helix | 14-18 | 5 | |
| α-helix | 24-31 | 8 | |
| α-helix | 34-41 | 8 | |
| α-helix | 93-95 | 3 | |
| β-strand | 99-102 | 4 | 1 |
| β-strand | 107-110 | 4 | 1 |
| β-strand | 115-117 | 3 | 2 |
| β-strand | 124-126 | 3 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Coagulation factor X precursor | L | protein | 138 | Homo sapiens | P00742 (AlphaFold model) |
| Coagulation factor X precursor | H | protein | 254 | Homo sapiens | P00742 (AlphaFold model) |
| Ecotin precursor | E | protein | 142 | Escherichia coli | P23827 (AlphaFold model) |
>1P0S_1 Coagulation factor X precursor (chains L) ANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGK CKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADN GKACIPTGPYPCGKQTLE
>1P0S_2 Coagulation factor X precursor (chains H) IVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTE QEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLM TQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDA CQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKA KSHAPEVITSSPLK
>1P0S_3 Ecotin precursor (chains E) AESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLE NKTLEGWGYDYYVFDKVSSPVSTRMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTP DNVDVKYRVWKAEEKIDNAVVR
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 4 |
Water and common crystallization additives (NA) are not listed.
The Extended Interactions and Gla Domain of Blood Coagulation Factor Xa. Wang, S.X., Hur, E., Sousa, C.A. et al. Biochemistry (2003) 42:7959-7966. DOI 10.1021/bi027320a · 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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