7pkh

C-reactive protein decamer at pH 5 with phosphocholine ligand

Method: ELECTRON MICROSCOPY Dmax: 134.2 Å Quality: GOOD

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

C-reactive protein

Homo sapiens

UniProt P02741

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 homooligomer Homooligomer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 19–224 Chain B; UniProt 19–224 Chain C; UniProt 19–224 Chain D; UniProt 19–224 Chain E; UniProt 19–224 Chain F; UniProt 19–224 Chain G; UniProt 19–224 Chain H; UniProt 19–224 Chain I; UniProt 19–224 Chain J; UniProt 19–224 Not recorded CA CALCIUM ION × 20 PC PHOSPHOCHOLINE × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 Å

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.

23 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–206; UniProt 19–224 Author chain B; PDBConstruct 1–206; UniProt 19–224 Author chain C; PDBConstruct 1–206; UniProt 19–224 Author chain D; PDBConstruct 1–206; UniProt 19–224 Author chain E; PDBConstruct 1–206; UniProt 19–224 Author chain F; PDBConstruct 1–206; UniProt 19–224 Author chain G; PDBConstruct 1–206; UniProt 19–224 Author chain H; PDBConstruct 1–206; UniProt 19–224 Author chain I; PDBConstruct 1–206; UniProt 19–224 Author chain J; PDBConstruct 1–206; UniProt 19–224

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 7pkh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7pkh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7pkh
Deposition date deposition_date2021-08-25
Structure title titleC-reactive protein decamer at pH 5 with phosphocholine ligand
Keywords keywordsC-reactive protein, CRP, immune system, innate immunity; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.24
Radius of gyration Rg (electron density) rg_electron41.38
Forward intensity I(0) i0742995000.00
Molecular weight molecular_weight233070.0 kDa
Excluded volume excluded_volume294890 ų
Envelope volume envelope_volume384530 ų
Hydration-shell volume shell_volume76584 ų
Envelope diameter envelope_diameter144.0
Shell Rg shell_rg47.97
Envelope Rg envelope_rg39.72
Shape Rg shape_rg41.32
Total Rg total_rg41.93
Total atoms total_atoms32520
Residues n_residues2060
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 dmax134.2
Rg (real space) rg_real42.03
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real7.4300e+08
I(0) uncertainty (real space) i0_real_error1.2400e+07
Rg (reciprocal space) rg_reciprocal42.23
I(0) (reciprocal space) i0_reciprocal743200000.0000
Solution quality estimate total_estimate0.8695
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.4
Skewness Skewness skewness0.148
Kurtosis Kurtosis kurtosis-0.312
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha78110000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.893

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)