4pjw

crystal structure of human Stromal Antigen 2 (SA2) in complex with Sister Chromatid Cohesion protein 1 (Scc1), with bound MES

Method: X-RAY DIFFRACTION Dmax: 130.9 Å Quality: GOOD

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

Cohesin subunit SA-2

Homo sapiens

UniProt Q8N3U4

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 80–1060 Fragment:UNP residues 80-1060 Non-standard monomer:Yes (specific site not provided by mmCIF) Double-strand-break repair protein rad21 homolog × 1 (O60216) MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.12 M Morpheus Divalents Mix, 0.1 M Morpheus Buffer System 1, and 27-30% (v/v) Morpheus EOD_P8K (Molecular Dimensions). Resolution 2.85 Å R-free 0.225

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.

8 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STAG2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–981; UniProt 80–1060

Double-strand-break repair protein rad21 homolog

Homo sapiens

UniProt O60216

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 281–420 Fragment:UNP residues 281-420 Non-standard monomer:Yes (specific site not provided by mmCIF) Cohesin subunit SA-2 × 1 (Q8N3U4) MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.12 M Morpheus Divalents Mix, 0.1 M Morpheus Buffer System 1, and 27-30% (v/v) Morpheus EOD_P8K (Molecular Dimensions). Resolution 2.85 Å R-free 0.225

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.

35 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAD21_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–140; UniProt 281–420

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 4pjw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4pjw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4pjw
Deposition date deposition_date2014-05-12
Structure title titlecrystal structure of human Stromal Antigen 2 (SA2) in complex with Sister Chromatid Cohesion protein 1 (Scc1), with bound MES
Keywords keywordsSister chromatid cohesion, cohesin subunits, protein-protein interaction, HEAT repeat, CELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.27
Radius of gyration Rg (electron density) rg_electron39.62
Forward intensity I(0) i0202257000.00
Molecular weight molecular_weight115540.0 kDa
Excluded volume excluded_volume144030 ų
Envelope volume envelope_volume202220 ų
Hydration-shell volume shell_volume42850 ų
Envelope diameter envelope_diameter138.0
Shell Rg shell_rg45.07
Envelope Rg envelope_rg38.94
Shape Rg shape_rg39.60
Total Rg total_rg40.00
Total atoms total_atoms15754
Residues n_residues944
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 dmax130.9
Rg (real space) rg_real40.31
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real2.0230e+08
I(0) uncertainty (real space) i0_real_error3.0420e+06
Rg (reciprocal space) rg_reciprocal40.27
I(0) (reciprocal space) i0_reciprocal202200000.0000
Solution quality estimate total_estimate0.8730
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.7
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.624
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16590000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.906; Smooth: 0.673

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)