SAXSdb — 1lqv

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Endothelial protein C receptor

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 18–210	Fragment：Extracellular domain	Vitamin-K dependent protein C × 1 （P04070） NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 CA CALCIUM ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；peg 400, potassium chloride, magnesium chloride, calcium chloride, hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.222
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 18–210	Fragment：Extracellular domain	Vitamin-K dependent protein C × 1 （P04070） NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 CA CALCIUM ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；peg 400, potassium chloride, magnesium chloride, calcium chloride, hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.222

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1LQV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1L8J Crystal Structure of the Endothelial Protein C Receptor and Bound Phospholipid Molecule Deposited 2002-03-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–210（193 aa） Fragment：Extracellular domain (residues 18-210)	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；Sodium Formate, TRIS-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.00 Å R-free 0.211
3JTC Importance of Mg2+ in the Ca2+-Dependent Folding of the gamma-Carboxyglutamic Acid Domains of Vitamin K-Dependent clotting and anticlotting Proteins Deposited 2009-09-11	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 18–210（193 aa） Fragment：extracellular domain (UNP residues 18-210)	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 MG MAGNESIUM ION × 2 CA CALCIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；PEG 400, potassium chloride, magnesium chloride, calcium chloride, HEPES, PH 7.0, VAPOR DIFFUSION	Resolution 1.60 Å R-free 0.226
3JTC Importance of Mg2+ in the Ca2+-Dependent Folding of the gamma-Carboxyglutamic Acid Domains of Vitamin K-Dependent clotting and anticlotting Proteins Deposited 2009-09-11	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 18–210（193 aa） Fragment：extracellular domain (UNP residues 18-210)	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 MG MAGNESIUM ION × 2 CA CALCIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；PEG 400, potassium chloride, magnesium chloride, calcium chloride, HEPES, PH 7.0, VAPOR DIFFUSION	Resolution 1.60 Å R-free 0.226
4V3D The CIDRa domain from HB3var03 PfEMP1 bound to endothelial protein C receptor Deposited 2014-10-17	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 25–194（170 aa） Fragment：EXTRACELLULAR DOMAIN, UNP RESIDUES 468-718	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.2 M NANO3, 0.1 M BTP PH 8.5, 20% PEG 3350	Resolution 2.65 Å R-free 0.255
4V3D The CIDRa domain from HB3var03 PfEMP1 bound to endothelial protein C receptor Deposited 2014-10-17	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 25–194（170 aa） Fragment：EXTRACELLULAR DOMAIN, UNP RESIDUES 468-718	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.2 M NANO3, 0.1 M BTP PH 8.5, 20% PEG 3350	Resolution 2.65 Å R-free 0.255
4V3E The CIDRa domain from IT4var07 PfEMP1 bound to endothelial protein C receptor Deposited 2014-10-17	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 25–195（171 aa）	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.2 M NANO3, 0.1 M BTP PH 7.5, 20% PEG 3350	Resolution 2.90 Å R-free 0.276
6SNY Synthetic mimic of an EPCR-binding PfEMP1 bound to EPCR Deposited 2019-08-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 18–210（193 aa）	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；2M sodium citrate, 0.1M HEPES pH 7	Resolution 3.11 Å R-free 0.256
6SNY Synthetic mimic of an EPCR-binding PfEMP1 bound to EPCR Deposited 2019-08-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain C 18–210（193 aa）	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；2M sodium citrate, 0.1M HEPES pH 7	Resolution 3.11 Å R-free 0.256
7OKS X-ray structure of soluble EPCR in P212121 space group Deposited 2021-05-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–210（193 aa）	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；2.8 M sodium acetate pH 8.0, 0.1 M Tris pH 7.0	Resolution 1.95 Å R-free 0.239
7OKS X-ray structure of soluble EPCR in P212121 space group Deposited 2021-05-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 18–210（193 aa）	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；2.8 M sodium acetate pH 8.0, 0.1 M Tris pH 7.0	Resolution 1.95 Å R-free 0.239
7OKS X-ray structure of soluble EPCR in P212121 space group Deposited 2021-05-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain C 18–210（193 aa）	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；2.8 M sodium acetate pH 8.0, 0.1 M Tris pH 7.0	Resolution 1.95 Å R-free 0.239
7OKS X-ray structure of soluble EPCR in P212121 space group Deposited 2021-05-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain D 18–210（193 aa）	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；2.8 M sodium acetate pH 8.0, 0.1 M Tris pH 7.0	Resolution 1.95 Å R-free 0.239
7OKT X-ray structure of soluble EPCR in C2221 space group Deposited 2021-05-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–210（193 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 EDO 1,2-ETHANEDIOL × 1 PTY PHOSPHATIDYLETHANOLAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；295 K；2.8 M Sodium acetate pH 7.0	Resolution 1.95 Å R-free 0.257
7OKT X-ray structure of soluble EPCR in C2221 space group Deposited 2021-05-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 18–210（193 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PTY PHOSPHATIDYLETHANOLAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；295 K；2.8 M Sodium acetate pH 7.0	Resolution 1.95 Å R-free 0.257
7OKU X-ray structure of soluble EPCR in P3121 space group Deposited 2021-05-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–210（193 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 EDO 1,2-ETHANEDIOL × 2 PTY PHOSPHATIDYLETHANOLAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；295 K；2.0 M Sodium formate, 0.1 M Sodium acetate pH 4.6	Resolution 1.95 Å R-free 0.235
7OKV Crystal structure of soluble EPCR after exposure to the nonionic surfactant Polysorbate 20 Deposited 2021-05-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–210（193 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 R16 HEXADECANE × 1 HEX HEXANE × 1 D10 DECANE × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；295 K；3.5 M Sodium formate, 0.1 M Sodium acetate pH 4.6	Resolution 1.85 Å R-free 0.234
7Q5D Structure of EPCR in a non-canonical conformation Deposited 2021-11-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–210（193 aa）	Not recorded	CYS CYSTEINE × 1 PTY PHOSPHATIDYLETHANOLAMINE × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.1 M sodium-potassium tartrate, 20% w/v PEG 3350	Resolution 1.80 Å R-free 0.195
8C44 HB3VAR03 apo headstructure (PfEMP1 A) complexed with EPCR Deposited 2022-12-31	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 26–193（168 aa）	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9TJX Structure of factor VII Gla domain bound to EPCR Deposited 2025-12-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 18–210（193 aa）	Not recorded	SO4 SULFATE ION × 2 PTY PHOSPHATIDYLETHANOLAMINE × 1 CA CALCIUM ION × 5 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.2 M Ammonium sulfate, 0.1 M Tris PH 8.5, 12 % w/v PEG 8000	Resolution 3.00 Å R-free 0.295
9TJX Structure of factor VII Gla domain bound to EPCR Deposited 2025-12-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 18–210（193 aa）	Not recorded	SO4 SULFATE ION × 2 PTY PHOSPHATIDYLETHANOLAMINE × 1 CA CALCIUM ION × 5 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.2 M Ammonium sulfate, 0.1 M Tris PH 8.5, 12 % w/v PEG 8000	Resolution 3.00 Å R-free 0.295
9TJX Structure of factor VII Gla domain bound to EPCR Deposited 2025-12-08	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 18–210（193 aa）	Not recorded	PTY PHOSPHATIDYLETHANOLAMINE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 5 MG MAGNESIUM ION × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.2 M Ammonium sulfate, 0.1 M Tris PH 8.5, 12 % w/v PEG 8000	Resolution 3.00 Å R-free 0.295
9TJX Structure of factor VII Gla domain bound to EPCR Deposited 2025-12-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 18–210（193 aa）	Not recorded	SO4 SULFATE ION × 1 PTY PHOSPHATIDYLETHANOLAMINE × 1 CA CALCIUM ION × 5 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.2 M Ammonium sulfate, 0.1 M Tris PH 8.5, 12 % w/v PEG 8000	Resolution 3.00 Å R-free 0.295

12 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	EPCR_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–193； UniProt 18–210 Author chain B； PDBConstruct 1–193； UniProt 18–210

Vitamin-K dependent protein C

Homo sapiens

UniProt P04070

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 43–75	Fragment：Protein C Gla domain Non-standard monomer：Yes (specific site not provided by mmCIF)	Endothelial protein C receptor × 1 （Q9UNN8） NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 CA CALCIUM ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；peg 400, potassium chloride, magnesium chloride, calcium chloride, hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.222
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 43–75	Fragment：Protein C Gla domain Non-standard monomer：Yes (specific site not provided by mmCIF)	Endothelial protein C receptor × 1 （Q9UNN8） NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 CA CALCIUM ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；peg 400, potassium chloride, magnesium chloride, calcium chloride, hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.222

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1LQV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AUT Human activated protein C Deposited 1996-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 212–461（250 aa） Chain L 84–197（114 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	0G6 D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.7；0.1 M CITRATE, 20% ISOPROPANOL 2% PEG 20000 PH 4.7	Resolution 2.80 Å
3F6U Crystal structure of human Activated Protein C (APC) complexed with PPACK Deposited 2008-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain H 212–451（240 aa） Fragment：UNP residues 212-451 Chain L 91–188（98 aa） Fragment：UNP residues 91-188	Not recorded	0G6 D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide × 1 NA SODIUM ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.236
3JTC Importance of Mg2+ in the Ca2+-Dependent Folding of the gamma-Carboxyglutamic Acid Domains of Vitamin K-Dependent clotting and anticlotting Proteins Deposited 2009-09-11	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 43–75（33 aa） Fragment：GLA domain (UNP residues 43-75)	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 MG MAGNESIUM ION × 2 CA CALCIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；PEG 400, potassium chloride, magnesium chloride, calcium chloride, HEPES, PH 7.0, VAPOR DIFFUSION	Resolution 1.60 Å R-free 0.226
3JTC Importance of Mg2+ in the Ca2+-Dependent Folding of the gamma-Carboxyglutamic Acid Domains of Vitamin K-Dependent clotting and anticlotting Proteins Deposited 2009-09-11	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 43–75（33 aa） Fragment：GLA domain (UNP residues 43-75)	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PTY PHOSPHATIDYLETHANOLAMINE × 1 MG MAGNESIUM ION × 2 CA CALCIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；PEG 400, potassium chloride, magnesium chloride, calcium chloride, HEPES, PH 7.0, VAPOR DIFFUSION	Resolution 1.60 Å R-free 0.226
4DT7 Crystal structure of thrombin bound to the activation domain QEDQVDPRLIDGKMTRRGDS of protein C Deposited 2012-02-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 204–223（20 aa） Fragment：UNP residues 204-223	Not recorded	NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.1 M Tris, pH 8.5, 0.2 M Na acetate, 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.90 Å R-free 0.218
4DT7 Crystal structure of thrombin bound to the activation domain QEDQVDPRLIDGKMTRRGDS of protein C Deposited 2012-02-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 204–223（20 aa） Fragment：UNP residues 204-223	Not recorded	NA SODIUM ION × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.1 M Tris, pH 8.5, 0.2 M Na acetate, 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.90 Å R-free 0.218
6M3B hAPC-c25k23 Fab complex Deposited 2020-03-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 212–461（250 aa） Chain D 43–197（155 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1% n-Octyl-beta-D-glucoside, 0.1M sodium citrate tribasic dehydrate pH 5.5, 22% (w/v) PEG 3350	Resolution 2.20 Å R-free 0.247
6M3C hAPC-h1573 Fab complex Deposited 2020-03-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 212–461（250 aa） Chain B 43–197（155 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.2M sodium fluoride, 20% (w/v) PEG 3350	Resolution 3.70 Å R-free 0.302
6M3C hAPC-h1573 Fab complex Deposited 2020-03-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 212–461（250 aa） Chain D 43–197（155 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.2M sodium fluoride, 20% (w/v) PEG 3350	Resolution 3.70 Å R-free 0.302
6M3C hAPC-h1573 Fab complex Deposited 2020-03-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 212–461（250 aa） Chain I 43–197（155 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.2M sodium fluoride, 20% (w/v) PEG 3350	Resolution 3.70 Å R-free 0.302
8JRU Cryo-EM structure of the glucagon receptor bound to beta-arrestin 1 in ligand-free state Deposited 2023-06-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 205–216（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8JRV Cryo-EM structure of the glucagon receptor bound to glucagon and beta-arrestin 1 Deposited 2023-06-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain R 205–216（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9BVM Vitamin K-dependent gamma-carboxylase with protein C propeptide and glutamate-rich region and with vitamin K hydroquinone Deposited 2024-05-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 19–88（70 aa）	Not recorded	A1AVC vitamin K1 hydroquinone × 1 6PL (4S,7R)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9MOT Cryo-EM structure of factor Va bound to activated protein C Deposited 2024-12-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 212–451（240 aa）	Mutation：S360A	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2 cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2, 40uM n-Dodecyl-B-D-Maltoside cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2 cryo-EM vitrification conditions Cryogen ETHANE cryo-EM vitrification conditions Cryogen ETHANE cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.15 Å
9MOV Cryo-EM structure of factor Va bound to activated protein C Deposited 2024-12-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 43–188（146 aa） Chain D 212–451（240 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S360A	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 CA CALCIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2 cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2, 40uM n-Dodecyl-B-D-Maltoside cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2 cryo-EM vitrification conditions Cryogen ETHANE cryo-EM vitrification conditions Cryogen ETHANE cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å

11 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PROC_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–33； UniProt 43–75 Author chain D； PDBConstruct 1–33； UniProt 43–75

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1lqv
Deposition date deposition_date	2002-05-13
Structure title title	Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C.
Keywords keywords	Gla (gamma-carboxyglutamic acid) residues, phospholipid binding groove, Ca ion binding, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	32.13 Å
Radius of gyration Rg (electron density) rg_electron	31.72 Å
Forward intensity I(0) i0	42654300.00
Molecular weight molecular_weight	51719.0 kDa
Excluded volume excluded_volume	64627 Å³
Envelope volume envelope_volume	85699 Å³
Hydration-shell volume shell_volume	23183 Å³
Envelope diameter envelope_diameter	109.2 Å
Shell Rg shell_rg	37.58 Å
Envelope Rg envelope_rg	31.15 Å
Shape Rg shape_rg	31.70 Å
Total Rg total_rg	32.30 Å
Total atoms total_atoms	3619
Residues n_residues	393
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	104.4 Å
Rg (real space) rg_real	32.38 Å
Rg uncertainty (real space) rg_real_error	1.05 Å
I(0) (real space) i0_real	4.2650e+07
I(0) uncertainty (real space) i0_real_error	7.4230e+05
Rg (reciprocal space) rg_reciprocal	32.28 Å
I(0) (reciprocal space) i0_reciprocal	42650000.0000
Solution quality estimate total_estimate	0.8406
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	25.6 Å
Skewness Skewness skewness	0.351
Kurtosis Kurtosis kurtosis	-0.696
Angular range angular_range	— – 0.2450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3871000.0000
Real-space data points n_real_points	50
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.728; Smooth: 0.704

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Endothelial protein C receptor
Molecular weight formula_weight	22046.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4048

SQDASDGLQRLHMLQISYFRDPYHVWYQGNASLGGHLTHVLEGPDTNTTIIQLQPLQEPESWARTQSGLQSYLLQFHGLVRLVHQERTLAFPLTIRCFLGCELPPEGSRAHVFFEVAVNGSSFVSFRPERALWQADTQVTSGVVTFTLQQLNAYNRTRYELREFLEDTCVQYVQKHISAENTKGSQTSRSYTS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Cricetulus griseus

Entity 2 Entity 2 polymer

Description description	Vitamin-K dependent protein C
Molecular weight formula_weight	4359.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

ANSFLEELRHSSLERECIEEICDFEEAKEIFQN

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606

Entity 3 Entity 3 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 4 Entity 4 non-polymer

Description description	PHOSPHATIDYLETHANOLAMINE
Molecular weight formula_weight	734.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	14

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	429

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1lqva_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.19 — MHC antigen-recognition domain
Superfamily Superfamily superfamily	d.19.1 — MHC antigen-recognition domain
Family Family family	d.19.1.1 — MHC antigen-recognition domain

Domain ID domain_id	d1lqvb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.19 — MHC antigen-recognition domain
Superfamily Superfamily superfamily	d.19.1 — MHC antigen-recognition domain
Family Family family	d.19.1.1 — MHC antigen-recognition domain

Domain ID domain_id	d1lqvc_
Class class	g — Small proteins
Fold Fold fold	g.32 — GLA-domain
Superfamily Superfamily superfamily	g.32.1 — GLA-domain
Family Family family	g.32.1.1 — GLA-domain

Domain ID domain_id	d1lqvd_
Class class	g — Small proteins
Fold Fold fold	g.32 — GLA-domain
Superfamily Superfamily superfamily	g.32.1 — GLA-domain
Family Family family	g.32.1.1 — GLA-domain

CATH v4.4 (2 domains)

Domain ID domain_id	1lqvA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — MHC class I-like antigen recognition-like

Domain ID domain_id	1lqvB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — MHC class I-like antigen recognition-like

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8. Citations (1)

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Unit-cell length a length_a	59.220 Å
Unit-cell length b length_b	62.360 Å
Unit-cell length c length_c	71.030 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	101.81 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.600 Å
Low-resolution limit resolution_low	12.000 Å
R factor r_factor	0.1890
R_work r_work	0.1890
R_free r_free	0.2220

fit	/app/data/saxs_computation/lq/1lqv/1lqv.fit
pddf	/app/data/pr_computation/lq/1lqv/1lqv.pr.out
profile	/app/data/saxs_computation/lq/1lqv/1lqv.dat

Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C.

1. Protein Identity and Related Structures Protein Identity & Related Structures

Endothelial protein C receptor

State in the Current Structure

Other States of the Same Protein in the Database

Vitamin-K dependent protein C

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)