7OKT: Soluble EPCR in C2221 space group

X-ray structure of soluble EPCR in C2221 space group. Determined by X-ray diffraction at 1.95 Å resolution. Released 27 Apr 2022.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,872
Mol. weight: 47.4 kDa
Ligands: PTY, NAG
Released: 27 Apr 2022

Explore 7OKT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7OKT contains 14 α-helices and 16 β-strands across 2 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.

Chain A: 8 helices, 8 β-strands

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	59-86	28
α-helix	88-90	3
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	155	1
α-helix	156-160	5
α-helix	161-163	3
α-helix	164-168	5
α-helix	169-176	8

Chain B: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	10-21	12	2
β-strand	24-33	10	2
β-strand	36-44	9	2
β-strand	49-52	4	2
α-helix	59-85	27
β-strand	93-102	10	2
β-strand	112-118	7	2
β-strand	121-127	7	2
β-strand	132-135	4	2
α-helix	146-151	6
α-helix	155-157	3
α-helix	159-163	5
α-helix	164-168	5
α-helix	169-176	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Endothelial protein C receptor	A, B	protein	195	Homo sapiens	Q9UNN8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7OKT_1 Endothelial protein C receptor (chains A, B)
GPSQDASDGLQRLHMLQISYFRDPYHVWYQGNASLGGHLTHVLEGPDTNTTIIQLQPLQE
PESWARTQSGLQSYLLQFHGLVRLVHQERTLAFPLTIRCFLGCELPPEGSRAHVFFEVAV
NGSSFVSFRPERALWQADTQVTSGVVTFTLQQLNAYNRTRYELREFLEDTCVQYVQKHIS
AENTKGSQTSRSYTS

Ligands and cofactors

ID	Name	Formula	Copies
PTY	Phosphatidylethanolamine	C40 H80 N O8 P	2
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	5

Water and common crystallization additives (EDO) are not listed.

Primary citation

Identification of a broad lipid repertoire associated to the endothelial cell protein C receptor (EPCR). Erausquin, E., Moran-Garrido, M., Saiz, J. et al. Sci Rep (2022) 12:15127-15127. DOI 10.1038/s41598-022-18844-y · PubMed

Other PDB entries of the same protein (UniProt Q9UNN8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1LQV 1.6 Å, Crystal structure of the Endothelial protein C receptor with phospholipid in the groove…
3JTC 1.6 Å, Importance of Mg2+ in the Ca2+-Dependent Folding of the gamma-Carboxyglutamic Acid…
7Q5D 1.8 Å, Structure of EPCR in a non-canonical conformation
7OKV 1.85 Å, Crystal structure of soluble EPCR after exposure to the nonionic surfactant Polysorbate 20
7OKS 1.95 Å, X-ray structure of soluble EPCR in P212121 space group
7OKU 1.95 Å, X-ray structure of soluble EPCR in P3121 space group
1L8J 2.0 Å, Crystal Structure of the Endothelial Protein C Receptor and Bound Phospholipid Molecule
4V3D 2.65 Å, The CIDRa domain from HB3var03 PfEMP1 bound to endothelial protein C receptor
4V3E 2.9 Å, The CIDRa domain from IT4var07 PfEMP1 bound to endothelial protein C receptor
9TJX 3.0 Å, Structure of factor VII Gla domain bound to EPCR
6SNY 3.11 Å, Synthetic mimic of an EPCR-binding PfEMP1 bound to EPCR
8C44 3.2 Å, HB3VAR03 apo headstructure (PfEMP1 A) complexed with EPCR

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