5ea0

Structure of the antibody 7968 with human complement factor H-derived peptide

Method: X-RAY DIFFRACTION Dmax: 81.6 Å Quality: EXCELLENT

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

Complement factor H-related protein 2

OrganismNot specified

UniProt P36980

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 P; UniProt 150–162 Fragment:UNP residues 150-162 Non-standard monomer:Yes (specific site not provided by mmCIF) Heavy chain of antibody 7968 Fab fragment × 1 Light chain of antibody 7968 Fab fragment × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 3.5;293 K;Drop composed of Fab at 20 mg/ml mixed with 25 mM citric acid pH 3.5, 8% PEG 3350; over a reservoir of 24% PEG 3350 Resolution 2.00 Å R-free 0.275

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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FHR2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 2–14; UniProt 150–162

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 5ea0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ea0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ea0
Deposition date deposition_date2015-10-15
Structure title titleStructure of the antibody 7968 with human complement factor H-derived peptide
Keywords keywordscomplement factor H CFH SCR19 SCR19-20, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.17
Radius of gyration Rg (electron density) rg_electron24.27
Forward intensity I(0) i039368900.00
Molecular weight molecular_weight48015.0 kDa
Excluded volume excluded_volume59811 ų
Envelope volume envelope_volume73046 ų
Hydration-shell volume shell_volume25433 ų
Envelope diameter envelope_diameter84.5
Shell Rg shell_rg31.21
Envelope Rg envelope_rg24.11
Shape Rg shape_rg24.26
Total Rg total_rg25.09
Total atoms total_atoms3380
Residues n_residues432
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 dmax81.6
Rg (real space) rg_real25.16
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real3.9370e+07
I(0) uncertainty (real space) i0_real_error5.4840e+05
Rg (reciprocal space) rg_reciprocal25.16
I(0) (reciprocal space) i0_reciprocal39370000.0000
Solution quality estimate total_estimate0.9013
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.8
Skewness Skewness skewness0.314
Kurtosis Kurtosis kurtosis-0.409
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7860000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5ea0H01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5ea0H02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5ea0L01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5ea0L02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)