3o2q

Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex

Method: X-RAY DIFFRACTION Dmax: 132.6 Å Quality: GOOD

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

Symplekin

Homo sapiens

UniProt Q92797

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 30–360 Fragment:N-terminal domain RNA polymerase II subunit A C-terminal domain phosphatase SSU72 × 1 (Q9NP77) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;1.6M ammonium chloride, 27% (w/v) PEG 3350, 10mM Sodium potassium tartrate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.40 Å R-free 0.242
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 30–360 Fragment:N-terminal domain RNA polymerase II subunit A C-terminal domain phosphatase SSU72 × 1 (Q9NP77) RNA polymerase II CTD Serine-5 phosphopeptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;1.6M ammonium chloride, 27% (w/v) PEG 3350, 10mM Sodium potassium tartrate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.40 Å R-free 0.242

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.

12 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYMPK_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 21–351; UniProt 30–360 Author chain D; PDBConstruct 21–351; UniProt 30–360

RNA polymerase II subunit A C-terminal domain phosphatase SSU72

Homo sapiens

UniProt Q9NP77

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 1–194 Mutation:C12S Symplekin × 1 (Q92797) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;1.6M ammonium chloride, 27% (w/v) PEG 3350, 10mM Sodium potassium tartrate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.40 Å R-free 0.242
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–194 Mutation:C12S Symplekin × 1 (Q92797) RNA polymerase II CTD Serine-5 phosphopeptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;1.6M ammonium chloride, 27% (w/v) PEG 3350, 10mM Sodium potassium tartrate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.40 Å R-free 0.242

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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SSU72_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 21–214; UniProt 1–194 Author chain E; PDBConstruct 21–214; UniProt 1–194

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 3o2q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3o2q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3o2q
Deposition date deposition_date2010-07-22
Structure title titleCrystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex
Keywords keywordsHeat repeat, scaffold, phosphatase, polymerase II CTD, cis-proline, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.68
Radius of gyration Rg (electron density) rg_electron38.49
Forward intensity I(0) i0204701000.00
Molecular weight molecular_weight115960.0 kDa
Excluded volume excluded_volume145370 ų
Envelope volume envelope_volume196260 ų
Hydration-shell volume shell_volume43369 ų
Envelope diameter envelope_diameter142.1
Shell Rg shell_rg43.02
Envelope Rg envelope_rg38.35
Shape Rg shape_rg38.49
Total Rg total_rg38.79
Total atoms total_atoms8132
Residues n_residues1014
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 dmax132.6
Rg (real space) rg_real38.78
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real2.0470e+08
I(0) uncertainty (real space) i0_real_error3.8190e+06
Rg (reciprocal space) rg_reciprocal38.73
I(0) (reciprocal space) i0_reciprocal204700000.0000
Solution quality estimate total_estimate0.8866
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.0
Skewness Skewness skewness0.303
Kurtosis Kurtosis kurtosis-0.560
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19960000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.924; Smooth: 0.967

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id3o2qA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id3o2qB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id3o2qB02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily550
Domain ID domain_id3o2qD00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id3o2qE01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id3o2qE02
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily550

8. Citations (1)

9. Files and Curves (10)