3m0c

The X-ray Crystal Structure of PCSK9 in Complex with the LDL receptor

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

Proprotein convertase subtilisin/kexin type 9

Homo sapiens

UniProt Q8NBP7

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 Low-density lipoprotein receptor × 1 (P01130) CALCIUM ION × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PCSK9_HUMAN
Isoform —
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–124; UniProt 29–152 Author chain B; PDBConstruct 1–540; UniProt 153–692

Low-density lipoprotein receptor

Homo sapiens

UniProt P01130

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 Proprotein convertase subtilisin/kexin type 9 × 1 (Q8NBP7) Proprotein convertase subtilisin/kexin type 9 × 1 (Q8NBP7) CALCIUM ION × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name LDLR_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–785; UniProt 4–788

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_id3m0c
Deposition date deposition_date2010-03-02
Structure title titleThe X-ray Crystal Structure of PCSK9 in Complex with the LDL receptor
Keywords keywords;PROTEIN COMPLEX, BETA PROPELLER, CHOLESTEROL CLEARANCE, PCSK9, LDLR, Autocatalytic cleavage, Cholesterol metabolism, Disease mutation, Disulfide bond, Glycoprotein, Hydrolase, Lipid metabolism, Phosphoprotein, Protease, Secreted, Serine protease, Steroid metabolism, Zymogen, Coated pit, EGF-like domain, Endocytosis, Host-virus interaction, LDL, Lipid transport, Membrane, Receptor, Transmembrane, Transport, PROTEIN BINDING ;; PROTEIN BINDING
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.

3m0c__assembly_1__model_1

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

Download this curve (.dat)

3m0c__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

3m0c__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)39.43 Å
Rg (electron density)39.18 Å
Total Rg39.50 Å
Atom count7690
Residues1008
Excluded volume135740 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3m0c__assembly_1__model_1 trimeric (3) 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 (4)

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7. Citations (1)