Structure of EPCR in a non-canonical conformation. Determined by X-ray diffraction at 1.8 Å resolution. Released 14 Sept 2022.
Explore 7Q5D in 3D Show helices and sheets RCSB PDB PDBe
7Q5D contains 5 α-helices and 8 β-strands across 1 chain. 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 | 10-21 | 12 | 1 |
| β-strand | 24-33 | 10 | 1 |
| β-strand | 36-44 | 9 | 1 |
| β-strand | 49-52 | 4 | 1 |
| α-helix | 59-87 | 29 | |
| β-strand | 93-102 | 10 | 1 |
| β-strand | 111-118 | 8 | 1 |
| β-strand | 121-127 | 7 | 1 |
| β-strand | 132-135 | 4 | 1 |
| α-helix | 142-151 | 10 | |
| α-helix | 156-163 | 8 | |
| α-helix | 164-169 | 6 | |
| α-helix | 170-176 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Endothelial protein C receptor | A | protein | 195 | Homo sapiens | Q9UNN8 (AlphaFold model) |
>7Q5D_1 Endothelial protein C receptor (chains A) GPSQDASDGLQRLHMLQISYFRDPYHVWYQGNASLGGHLTHVLEGPDTNTTIIQLQPLQE PESWARTQSGLQSYLLQFHGLVRLVHQERTLAFPLTIRCFLGCELPPEGSRAHVFFEVAV NGSSFVSFRPERALWQADTQVTSGVVTFTLQQLNAYNRTRYELREFLEDTCVQYVQKHIS AENTKGSQTSRSYTS
Water and common crystallization additives (GOL) are not listed.
Structural vulnerability in EPCR suggests functional modulation. Erausquin, E., Rodriguez-Fernandez, A., Rodriguez-Lumbreras, L.A. et al. Sci Rep (2024) 14:2591-2591. DOI 10.1038/s41598-024-53160-7 · PubMed
Other PDB entries of the same protein (UniProt Q9UNN8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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