1lqv

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

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Endothelial protein C receptor

Homo sapiens

UniProt Q9UNN8

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Vitamin-K dependent protein C × 1 (P04070) 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PHOSPHATIDYLETHANOLAMINE × 1 CALCIUM ION × 7 water × 2 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 Vitamin-K dependent protein C × 1 (P04070) 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PHOSPHATIDYLETHANOLAMINE × 1 CALCIUM ION × 7 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Endothelial protein C receptor × 1 (Q9UNN8) 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PHOSPHATIDYLETHANOLAMINE × 1 CALCIUM ION × 7 water × 2 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 Endothelial protein C receptor × 1 (Q9UNN8) 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PHOSPHATIDYLETHANOLAMINE × 1 CALCIUM ION × 7 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

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_id1lqv
Deposition date deposition_date2002-05-13
Structure title titleCrystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C.
Keywords keywordsGla (gamma-carboxyglutamic acid) residues, phospholipid binding groove, Ca ion binding, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1lqv__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1lqv__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1lqv__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)19.69 Å
Rg (electron density)18.51 Å
Total Rg19.51 Å
Atom count1804
Residues196
Excluded volume32212 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1lqv__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1lqv__assembly_2__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (6)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1lqva_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.19 — MHC antigen-recognition domain
Superfamily Superfamily superfamilyd.19.1 — MHC antigen-recognition domain
Family Family familyd.19.1.1 — MHC antigen-recognition domain
Domain ID domain_idd1lqvb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.19 — MHC antigen-recognition domain
Superfamily Superfamily superfamilyd.19.1 — MHC antigen-recognition domain
Family Family familyd.19.1.1 — MHC antigen-recognition domain
Domain ID domain_idd1lqvc_
Class classg — Small proteins
Fold Fold foldg.32 — GLA-domain
Superfamily Superfamily superfamilyg.32.1 — GLA-domain
Family Family familyg.32.1.1 — GLA-domain
Domain ID domain_idd1lqvd_
Class classg — Small proteins
Fold Fold foldg.32 — GLA-domain
Superfamily Superfamily superfamilyg.32.1 — GLA-domain
Family Family familyg.32.1.1 — GLA-domain

CATH v4.4 (2 domains)

Domain ID domain_id1lqvA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily10 — MHC class I-like antigen recognition-like
Domain ID domain_id1lqvB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily10 — MHC class I-like antigen recognition-like
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7. Citations (1)