6hkw

Crystal structure of human SDS22

Method: X-RAY DIFFRACTION Dmax: 152.8 Å Quality: REASONABLE

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

Protein phosphatase 1 regulatory subunit 7

Homo sapiens

UniProt Q15435

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 1–360 Not recorded SO4 SULFATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;ammonium sulfate, PEG 4000, glycerol Resolution 3.09 Å R-free 0.239
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–360 Not recorded SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;ammonium sulfate, PEG 4000, glycerol Resolution 3.09 Å R-free 0.239
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–360 Not recorded SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;ammonium sulfate, PEG 4000, glycerol Resolution 3.09 Å R-free 0.239
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–360 Not recorded SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;ammonium sulfate, PEG 4000, glycerol Resolution 3.09 Å R-free 0.239
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 1–360 Not recorded SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;ammonium sulfate, PEG 4000, glycerol Resolution 3.09 Å R-free 0.239

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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PP1R7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–363; UniProt 1–360 Author chain B; PDBConstruct 4–363; UniProt 1–360 Author chain C; PDBConstruct 4–363; UniProt 1–360 Author chain D; PDBConstruct 4–363; UniProt 1–360 Author chain E; PDBConstruct 4–363; UniProt 1–360

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 6hkw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6hkw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6hkw
Deposition date deposition_date2018-09-09
Structure title titleCrystal structure of human SDS22
Keywords keywordsLRR protein, signaling protein, PP1 regulator; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.66
Radius of gyration Rg (electron density) rg_electron45.51
Forward intensity I(0) i0485077000.00
Molecular weight molecular_weight179530.0 kDa
Excluded volume excluded_volume224470 ų
Envelope volume envelope_volume321160 ų
Hydration-shell volume shell_volume60082 ų
Envelope diameter envelope_diameter154.5
Shell Rg shell_rg48.76
Envelope Rg envelope_rg44.55
Shape Rg shape_rg45.52
Total Rg total_rg45.65
Total atoms total_atoms12575
Residues n_residues1530
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 dmax152.8
Rg (real space) rg_real45.66
Rg uncertainty (real space) rg_real_error1.75
I(0) (real space) i0_real4.8510e+08
I(0) uncertainty (real space) i0_real_error1.0310e+07
Rg (reciprocal space) rg_reciprocal45.66
I(0) (reciprocal space) i0_reciprocal485100000.0000
Solution quality estimate total_estimate0.6590
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.4
Skewness Skewness skewness0.269
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23390000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 0.010; Positv: 1.000; Valcen: 0.984; Smooth: 0.845

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)