4b2s

Solution structure of CCP modules 11-12 of complement factor H

Method: SOLUTION NMR Dmax: 73.9 Å Quality: REASONABLE

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 627–747 Fragment:CCPS 11-12, RESIDUES 627-747 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.3;298 K;Ionic strength (raw mmCIF value) 0.02;Pressure 1.0 NMR measurement conditions:pH 6.3;298 K;Ionic strength (raw mmCIF value) 0.02;Pressure 1.0 NMR sample composition:90% H2O/10% D2O Resolution not provided

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 7–127; UniProt 627–747

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 4b2s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4b2s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4b2s
Deposition date deposition_date2012-07-17
Structure title titleSolution structure of CCP modules 11-12 of complement factor H
Keywords keywordsIMMUNE SYSTEM, SAXS, SHORT CONSENSUS REPEAT; IMMUNE SYSTEM
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.59
Radius of gyration Rg (electron density) rg_electron19.55
Forward intensity I(0) i01166010000.00
Molecular weight molecular_weight281800.0 kDa
Excluded volume excluded_volume347990 ų
Envelope volume envelope_volume36298 ų
Hydration-shell volume shell_volume14318 ų
Envelope diameter envelope_diameter81.4
Shell Rg shell_rg27.83
Envelope Rg envelope_rg24.52
Shape Rg shape_rg19.57
Total Rg total_rg19.63
Total atoms total_atoms38220
Residues n_residues2540
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 dmax73.9
Rg (real space) rg_real19.93
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real1.1660e+09
I(0) uncertainty (real space) i0_real_error1.6020e+07
Rg (reciprocal space) rg_reciprocal19.88
I(0) (reciprocal space) i0_reciprocal1166000000.0000
Solution quality estimate total_estimate0.7129
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.6
Skewness Skewness skewness0.521
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha266900.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.451; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.095; Smooth: 0.817

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4b2sA01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1
Domain ID domain_id4b2sA02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1

8. Citations (1)

9. Files and Curves (10)