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2kkr

Solution structure of SCA7 zinc finger domain from human ataxin-7 protein

Method: SOLUTION NMR Dmax: 34.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Ataxin-7

Homo sapiens

UniProt O15265

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 330–401 Fragment：residues 339-397 ZN ZINC ION × 1 SOLUTION NMR NMR measurement conditions：pH 7.1；295 K；Ionic strength (raw mmCIF value) 0.3；Pressure ambient NMR sample composition：50 mM sodium phosphate, 200 mM sodium chloride, 2 mM DTT, 0.3 mM [U-99% 13C; U-99% 15N] ATXN7, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：50 mM sodium phosphate, 200 mM sodium chloride, 2 mM DTT, 0.6 mM ATXN7, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

Other PDB Difference from Current Entry 2KKR Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7KTR Cryo-EM structure of the human SAGA coactivator complex (TRRAP, core) Deposited 2020-11-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric
Chain N 1–892（892 aa）
Not recorded IHP INOSITOL HEXAKISPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8；Buffers were freshly prepared and 0.22 um filtered.
cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, blot time 3 sec
Resolution 2.93 Å
7KTS Negative stain EM structure of the human SAGA coactivator complex (TRRAP, core, splicing module) Deposited 2020-11-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: tridecameric
Chain N 1–892（892 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；Buffers were freshly prepared and 0.22 um filtered.
Resolution 19.09 Å
8H7G Cryo-EM structure of the human SAGA complex Deposited 2022-10-20 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric
Chain L 1–892（892 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å
9RDK Cryo-EM structure of the human SAGA co-activator complex Deposited 2025-06-03 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: 13-meric
Chain N 1–892（892 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.41 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATX7_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–74； UniProt 330–401

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 2kkr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2kkr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2kkr
Deposition date deposition_date2009-06-29
Structure title titleSolution structure of SCA7 zinc finger domain from human ataxin-7 protein
Keywords keywordsStructural Genomics, Structural Proteomics in Europe, Zinc Finger, SPINE, transcription, PROTEIN BINDING; TRANSCRIPTION, PROTEIN BINDING
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier10.83 Å
Radius of gyration Rg (electron density) rg_electron10.92 Å
Forward intensity I(0) i0321737000.00
Molecular weight molecular_weight140350.0 kDa
Excluded volume excluded_volume171890 ų
Envelope volume envelope_volume14474 ų
Hydration-shell volume shell_volume10015 ų
Envelope diameter envelope_diameter41.2 Å
Shell Rg shell_rg17.94 Å
Envelope Rg envelope_rg12.84 Å
Shape Rg shape_rg10.93 Å
Total Rg total_rg11.06 Å
Total atoms total_atoms19720
Residues n_residues1180
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax34.6 Å
Rg (real space) rg_real10.78 Å
Rg uncertainty (real space) rg_real_error0.28 Å
I(0) (real space) i0_real3.2170e+08
I(0) uncertainty (real space) i0_real_error3.2820e+06
Rg (reciprocal space) rg_reciprocal10.79 Å
I(0) (reciprocal space) i0_reciprocal321700000.0000
Solution quality estimate total_estimate0.8987
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.0 Å
Skewness Skewness skewness0.176
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46380.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.960
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2kkrA01
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily670 —
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8. Citations (1)

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9. Files and Curves (10)