5c7f

Crystal structure of the rice Topless related protein 2 (TPR2) N-terminal domain (1-209) in complex with Arabidopsis IAA1 peptide

Method: X-RAY DIFFRACTION Dmax: 143.7 Å Quality: GOOD

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

ASPR2 protein

Oryza sativa

UniProt Q5NBT9

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–209 Chain B; UniProt 1–209 Chain C; UniProt 1–209 Chain D; UniProt 1–209 Fragment:N-terminal domain (UNP residues 1-209) Auxin-responsive protein IAA1 × 4 (P49677) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;25% w/v PEG 3,350, 0.2 M NaCl, 0.1 M BIS-TRIS pH 5.5 Resolution 2.70 Å R-free 0.256

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 Q5NBT9_ORYSJ
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–209; UniProt 1–209 Author chain B; PDBConstruct 1–209; UniProt 1–209 Author chain C; PDBConstruct 1–209; UniProt 1–209 Author chain D; PDBConstruct 1–209; UniProt 1–209

Auxin-responsive protein IAA1

OrganismNot specified

UniProt P49677

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 10–20 Chain F; UniProt 10–20 Chain G; UniProt 10–20 Chain H; UniProt 10–20 Fragment:UNP residues 10-20 ASPR2 protein × 4 (Q5NBT9) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;25% w/v PEG 3,350, 0.2 M NaCl, 0.1 M BIS-TRIS pH 5.5 Resolution 2.70 Å R-free 0.256

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 IAA1_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–11; UniProt 10–20 Author chain F; PDBConstruct 1–11; UniProt 10–20 Author chain G; PDBConstruct 1–11; UniProt 10–20 Author chain H; PDBConstruct 1–11; UniProt 10–20

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 5c7f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5c7f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5c7f
Deposition date deposition_date2015-06-24
Structure title titleCrystal structure of the rice Topless related protein 2 (TPR2) N-terminal domain (1-209) in complex with Arabidopsis IAA1 peptide
Keywords keywords;transcriptional corepressor, alpha-helical structure, tetrameric protein, plant transcriptional repression, TRANSCRIPTION, Plant development, auxin signaling ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.61
Radius of gyration Rg (electron density) rg_electron38.60
Forward intensity I(0) i0133533000.00
Molecular weight molecular_weight96932.0 kDa
Excluded volume excluded_volume122910 ų
Envelope volume envelope_volume164580 ų
Hydration-shell volume shell_volume38135 ų
Envelope diameter envelope_diameter153.0
Shell Rg shell_rg40.96
Envelope Rg envelope_rg38.28
Shape Rg shape_rg38.54
Total Rg total_rg38.97
Total atoms total_atoms6841
Residues n_residues825
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 dmax143.7
Rg (real space) rg_real39.18
Rg uncertainty (real space) rg_real_error1.73
I(0) (real space) i0_real1.3350e+08
I(0) uncertainty (real space) i0_real_error2.5720e+06
Rg (reciprocal space) rg_reciprocal38.82
I(0) (reciprocal space) i0_reciprocal133500000.0000
Solution quality estimate total_estimate0.7966
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.6
Skewness Skewness skewness0.685
Kurtosis Kurtosis kurtosis0.264
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9843000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.604; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.769; Smooth: 0.770

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)