2w2p

PCSK9-deltaC D374A mutant bound to WT EGF-A of LDLR

Method: X-RAY DIFFRACTION Dmax: 89.4 Å Quality: REASONABLE

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 153–451 Chain P; UniProt 53–152 Fragment:CATALYTIC DOMAIN, RESIDUES 153-451 Mutation:YES Fragment:PRODOMAIN, RESIDUES 53-152 LOW-DENSITY LIPOPROTEIN RECEPTOR × 1 (P01130) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1M HEPES PH 7.5, 10% (W/V) PEG 8000 AND 8% (V/V) ETHYLENE GLYCOL Resolution 2.62 Å R-free 0.270

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.

63 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCSK9_HUMAN
Isoform
PDB entities 1, 3
Chains and sequence ranges Author chain A; PDBConstruct 1–299; UniProt 153–451 Author chain P; PDBConstruct 15–114; UniProt 53–152

LOW-DENSITY LIPOPROTEIN RECEPTOR

HOMO SAPIENS

UniProt P01130

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 314–393 Fragment:EGF-A DOMAIN, RESIDUES 314-393 PROPROTEIN CONVERTASE SUBTILISIN/KEXIN TYPE 9 × 1 (Q8NBP7) PROPROTEIN CONVERTASE SUBTILISIN/KEXIN TYPE 9 × 1 (Q8NBP7) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1M HEPES PH 7.5, 10% (W/V) PEG 8000 AND 8% (V/V) ETHYLENE GLYCOL Resolution 2.62 Å R-free 0.270

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.

33 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LDLR_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 28–107; UniProt 314–393

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.

SAXS scattering curve SAXS Profile

SAXS profile for 2w2p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2w2p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2w2p
Deposition date deposition_date2008-11-03
Structure title titlePCSK9-deltaC D374A mutant bound to WT EGF-A of LDLR
Keywords keywords;HYDROLASE-RECEPTOR COMPLEX, PCSK9, LDLR, PROPROTEIN CONVERTASE, LOW-DENSITY LIPOPROTEIN RECEPTOR, EGF, CARDIOVASCULAR DISEASE, FAMILIAL HYPERCHOLESTEROLEMIA, LIPID METABOLISM, SERINE PROTEASE, HYDROLASE, LIPID TRANSPORT, STEROID METABOLISM, RECEPTOR ;; HYDROLASE/RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.68
Radius of gyration Rg (electron density) rg_electron22.83
Forward intensity I(0) i034946000.00
Molecular weight molecular_weight44617.0 kDa
Excluded volume excluded_volume55537 ų
Envelope volume envelope_volume67166 ų
Hydration-shell volume shell_volume24937 ų
Envelope diameter envelope_diameter95.0
Shell Rg shell_rg29.78
Envelope Rg envelope_rg23.59
Shape Rg shape_rg22.81
Total Rg total_rg23.71
Total atoms total_atoms3128
Residues n_residues415
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax89.4
Rg (real space) rg_real23.73
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real3.4950e+07
I(0) uncertainty (real space) i0_real_error5.1320e+05
Rg (reciprocal space) rg_reciprocal23.72
I(0) (reciprocal space) i0_reciprocal34950000.0000
Solution quality estimate total_estimate0.6170
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9
Skewness Skewness skewness0.470
Kurtosis Kurtosis kurtosis0.007
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7623000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.583; Stabil: 1.000; Sysdev: 0.154; Positv: 1.000; Valcen: 0.830; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2w2pa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.41 — Subtilisin-like
Superfamily Superfamily superfamilyc.41.1 — Subtilisin-like
Family Family familyc.41.1.1 — Subtilases
Domain ID domain_idd2w2pe1
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.0 — automated matches
Domain ID domain_idd2w2pe2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id2w2pA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily200 — Peptidase S8/S53 domain
Domain ID domain_id2w2pE00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin
Domain ID domain_id2w2pP01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily80 — Peptidase S8 propeptide/proteinase inhibitor I9

8. Citations (1)

9. Files and Curves (10)