9ydf

Structure of the cyclic nucleotide binding domain of SLC9C1

Method: X-RAY DIFFRACTION Dmax: 47.5 Å Quality: EXCELLENT

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

Solute carrier family 9 member C1

Homo sapiens

UniProt Q4G0N8

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 859–1013 Not recorded EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;20% (w/v) polyethylene glycol (PEG) 3350, 0.2 M Calcium chloride dihydrate Resolution 2.18 Å R-free 0.237

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name SL9C1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 19–173; UniProt 859–1013

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 9ydf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ydf
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9ydf
Deposition date deposition_date2025-09-22
最后修订 last_revision2025-11-12
Structure title titleStructure of the cyclic nucleotide binding domain of SLC9C1
Keywords keywords;Transporter, cyclic nucleotide binding domain, sperm-specific protein, SGC, TRANSPORT PROTEIN, Structural Genomics, PSI-2, Protein Structure Initiative, Structural Genomics Consortium ;; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.71
Radius of gyration Rg (electron density) rg_electron14.31
Forward intensity I(0) i03788760.00
Molecular weight molecular_weight14494.0 kDa
Excluded volume excluded_volume18445 ų
Envelope volume envelope_volume20682 ų
Hydration-shell volume shell_volume12379 ų
Envelope diameter envelope_diameter45.9
Shell Rg shell_rg19.87
Envelope Rg envelope_rg14.49
Shape Rg shape_rg14.31
Total Rg total_rg15.50
Total atoms total_atoms1017
Residues n_residues131
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 dmax47.5
Rg (real space) rg_real15.60
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real3.7890e+06
I(0) uncertainty (real space) i0_real_error3.8670e+04
Rg (reciprocal space) rg_reciprocal15.61
I(0) (reciprocal space) i0_reciprocal3789000.0000
Solution quality estimate total_estimate0.9091
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.9
Skewness Skewness skewness0.056
Kurtosis Kurtosis kurtosis-0.500
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha388300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)