1haq

FOUR MODELS OF HUMAN FACTOR H DETERMINED BY SOLUTION SCATTERING CURVE-FITTING AND HOMOLOGY MODELLING

Method: SOLUTION SCATTERING Dmax: 424.4 Å Quality: GOOD

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

COMPLEMENT FACTOR H

OrganismNot specified

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 19–1231 Not recorded No other associated polymer SOLUTION SCATTERING mmCIF provides none of the parsed experimental conditions 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 1–1213; UniProt 19–1231

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 1haq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1haq
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1haq
Deposition date deposition_date2001-04-06
Structure title titleFOUR MODELS OF HUMAN FACTOR H DETERMINED BY SOLUTION SCATTERING CURVE-FITTING AND HOMOLOGY MODELLING
Keywords keywordsIMMUNOLOGY, COMPLEMENT, GLYCOPROTEIN, COMPLEMENT ALTERNATE PATHWAY, SCR, CCP; GLYCOPROTEIN
Experimental Method methodSOLUTION SCATTERING

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron146.60
Forward intensity I(0) i04517770000.00
Molecular weight molecular_weight548330.0 kDa
Excluded volume excluded_volume658450 ų
Envelope volume envelope_volume1746200 ų
Hydration-shell volume shell_volume116100 ų
Envelope diameter envelope_diameter536.3
Shell Rg shell_rg104.60
Envelope Rg envelope_rg141.90
Shape Rg shape_rg146.40
Total Rg total_rg146.40
Total atoms total_atoms
Residues n_residues
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 dmax424.4
Rg (real space) rg_real140.50
Rg uncertainty (real space) rg_real_error2.49
I(0) (real space) i0_real4.3870e+09
I(0) uncertainty (real space) i0_real_error1.0900e+08
Rg (reciprocal space) rg_reciprocal123.20
I(0) (reciprocal space) i0_reciprocal4157000000.0000
Solution quality estimate total_estimate0.8897
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary169.8
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.560
Angular range angular_range— – 0.0500 −1
Current regularization parameter α current_alpha1.1290
Highest regularization parameter α highest_alpha595100000.0000
Real-space data points n_real_points11
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.040; Oscil: 0.963; Stabil: 0.945; Sysdev: 1.000; Positv: 1.000; Valcen: 0.844; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)