1a1g

DSNR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCGT SITE)

Method: X-RAY DIFFRACTION Dmax: 54.0 Å Quality: GOOD

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

DSNR ZINC FINGER PEPTIDE

Mus musculus

UniProt P08046

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–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 308–396 Not recorded ;DNA (5'-D(*AP*GP*CP*GP*TP*GP*GP*GP*CP*GP*T)-3') ; × 1 ;DNA (5'-D(*TP*AP*CP*GP*CP*CP*CP*AP*CP*GP*C)-3') ; × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;25% PEG 1450, 200 MM NACL, 25 MM BIS-TRIS PROPANE PH 8.0, VAPOR DIFFUSION, HANGING DROP Resolution 1.90 Å R-free 0.275

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.

15 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EGR1_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 2–90; UniProt 308–396

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 1a1g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a1g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a1g
Deposition date deposition_date1997-12-10
Structure title titleDSNR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCGT SITE)
Keywords keywordsCOMPLEX (ZINC FINGER-DNA), ZINC FINGER, DNA-BINDING PROTEIN, TRANSCRIPTION-DNA COMPLEX; TRANSCRIPTION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.90
Radius of gyration Rg (electron density) rg_electron15.66
Forward intensity I(0) i09168380.00
Molecular weight molecular_weight16836.0 kDa
Excluded volume excluded_volume18646 ų
Envelope volume envelope_volume22973 ų
Hydration-shell volume shell_volume12869 ų
Envelope diameter envelope_diameter55.8
Shell Rg shell_rg20.84
Envelope Rg envelope_rg15.97
Shape Rg shape_rg15.59
Total Rg total_rg16.54
Total atoms total_atoms1143
Residues n_residues106
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 dmax54.0
Rg (real space) rg_real15.86
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real9.1680e+06
I(0) uncertainty (real space) i0_real_error1.0490e+05
Rg (reciprocal space) rg_reciprocal15.87
I(0) (reciprocal space) i0_reciprocal9168000.0000
Solution quality estimate total_estimate0.7838
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.8
Skewness Skewness skewness0.327
Kurtosis Kurtosis kurtosis-0.168
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1280000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.738; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1a1ga1
Class classg — Small proteins
Fold Fold foldg.37 — beta-beta-alpha zinc fingers
Superfamily Superfamily superfamilyg.37.1 — beta-beta-alpha zinc fingers
Family Family familyg.37.1.1 — Classic zinc finger, C2H2
Domain ID domain_idd1a1ga2
Class classg — Small proteins
Fold Fold foldg.37 — beta-beta-alpha zinc fingers
Superfamily Superfamily superfamilyg.37.1 — beta-beta-alpha zinc fingers
Family Family familyg.37.1.1 — Classic zinc finger, C2H2
Domain ID domain_idd1a1ga3
Class classg — Small proteins
Fold Fold foldg.37 — beta-beta-alpha zinc fingers
Superfamily Superfamily superfamilyg.37.1 — beta-beta-alpha zinc fingers
Family Family familyg.37.1.1 — Classic zinc finger, C2H2

CATH v4.4 (3 domains)

Domain ID domain_id1a1gA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily60 — Classic Zinc Finger
Domain ID domain_id1a1gA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily60 — Classic Zinc Finger
Domain ID domain_id1a1gA03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily60 — Classic Zinc Finger

8. Citations (4)

9. Files and Curves (10)