9x1h

Cryo-EM Structure of human complement C1s CUB domain in complex with RAY121

Method: ELECTRON MICROSCOPY Dmax: 106.0 Å Quality: GOOD

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

Complement C1s subcomponent heavy chain

Homo sapiens

UniProt P09871

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 16–292 Chain B; UniProt 16–292 Not recorded RAY121 Fab Light chain × 2 RAY121 Fab Heavy chain × 2 CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20mM HEPES(7.5), 150mM NaCl, 3mM CaCl2, 0.03% DDM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

13 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C1S_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–277; UniProt 16–292 Author chain B; PDBConstruct 1–277; UniProt 16–292

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 9x1h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x1h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9x1h
Deposition date deposition_date2025-10-02
最后修订 last_revision2025-11-19
Structure title titleCryo-EM Structure of human complement C1s CUB domain in complex with RAY121
Keywords keywordsPH-DEPENDENT, RECYCLING ANTIBODY, IMMUNE SYSTEM, COMPLEMENT C1s, FAB, COMPLEX, CUB DOMAIN, EGF-LIKE DOMAIN; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.50
Radius of gyration Rg (electron density) rg_electron31.98
Forward intensity I(0) i0115037000.00
Molecular weight molecular_weight83577.0 kDa
Excluded volume excluded_volume103490 ų
Envelope volume envelope_volume134000 ų
Hydration-shell volume shell_volume35369 ų
Envelope diameter envelope_diameter110.7
Shell Rg shell_rg38.56
Envelope Rg envelope_rg31.33
Shape Rg shape_rg31.96
Total Rg total_rg32.59
Total atoms total_atoms5888
Residues n_residues754
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 dmax106.0
Rg (real space) rg_real32.52
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real1.1500e+08
I(0) uncertainty (real space) i0_real_error1.7880e+06
Rg (reciprocal space) rg_reciprocal32.52
I(0) (reciprocal space) i0_reciprocal115000000.0000
Solution quality estimate total_estimate0.8943
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.6
Skewness Skewness skewness0.292
Kurtosis Kurtosis kurtosis-0.487
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14310000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)