4k12

Structural Basis for Host Specificity of Factor H Binding by Streptococcus pneumoniae

Method: X-RAY DIFFRACTION Dmax: 61.3 Å Quality: GOOD

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

Complement factor H

Homo sapiens

UniProt P08603

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 508–567 Fragment:sushi domain (UNP residues 508-567) Choline binding protein A × 1 (G6W2B2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;20% PEG3500, 0.1 M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;20% PEG3500, 0.1 M sodium acetate, soaked in 0.5 M sodium iodide, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.08 Å R-free 0.170

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.

47 other PDB entries and 75 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CFAH_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–64; UniProt 508–567

Choline binding protein A

Streptococcus pneumoniae

UniProt G6W2B2

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 B; UniProt 68–148 Fragment:UNP residues 68-148 Complement factor H × 1 (P08603) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;20% PEG3500, 0.1 M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;20% PEG3500, 0.1 M sodium acetate, soaked in 0.5 M sodium iodide, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.08 Å R-free 0.170

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G6W2B2_STREE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–84; UniProt 68–148

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 4k12

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4k12
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4k12
Deposition date deposition_date2013-04-04
Structure title titleStructural Basis for Host Specificity of Factor H Binding by Streptococcus pneumoniae
Keywords keywordsprotein-protein complex, Complement-binding complex, IMMUNE SYSTEM-CHOLINE BINDING PROTEIN complex; IMMUNE SYSTEM/CHOLINE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.78
Radius of gyration Rg (electron density) rg_electron16.78
Forward intensity I(0) i05556900.00
Molecular weight molecular_weight16432.0 kDa
Excluded volume excluded_volume20284 ų
Envelope volume envelope_volume24276 ų
Hydration-shell volume shell_volume12886 ų
Envelope diameter envelope_diameter56.9
Shell Rg shell_rg21.69
Envelope Rg envelope_rg16.99
Shape Rg shape_rg16.73
Total Rg total_rg17.78
Total atoms total_atoms1150
Residues n_residues146
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 dmax61.3
Rg (real space) rg_real17.80
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real5.5570e+06
I(0) uncertainty (real space) i0_real_error7.8460e+04
Rg (reciprocal space) rg_reciprocal17.80
I(0) (reciprocal space) i0_reciprocal5557000.0000
Solution quality estimate total_estimate0.7874
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.2
Skewness Skewness skewness0.354
Kurtosis Kurtosis kurtosis-0.357
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1851000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.778; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.913; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4k12A00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id4k12B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology81 — Receptor-associated Protein
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)