1a1h

QGSR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCAC SITE)

Method: X-RAY DIFFRACTION Dmax: 56.9 Å Quality: REASONABLE

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

QGSR 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*AP*C)-3') ; × 1 ;DNA (5'-D(*TP*GP*TP*GP*CP*CP*CP*AP*CP*GP*C)-3') ; × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;27.5-35% PEG 3350, 0-200 MM NACL, 100 MM TRIS PH 8.5, VAPOR DIFFUSION Resolution 1.60 Å R-free 0.277

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 1a1h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a1h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a1h
Deposition date deposition_date1997-12-10
Structure title titleQGSR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCAC 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_guinier16.23
Radius of gyration Rg (electron density) rg_electron15.98
Forward intensity I(0) i09223240.00
Molecular weight molecular_weight16950.0 kDa
Excluded volume excluded_volume18801 ų
Envelope volume envelope_volume23813 ų
Hydration-shell volume shell_volume13075 ų
Envelope diameter envelope_diameter60.5
Shell Rg shell_rg21.31
Envelope Rg envelope_rg16.44
Shape Rg shape_rg15.90
Total Rg total_rg16.88
Total atoms total_atoms1151
Residues n_residues107
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 dmax56.9
Rg (real space) rg_real16.22
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real9.2230e+06
I(0) uncertainty (real space) i0_real_error1.1050e+05
Rg (reciprocal space) rg_reciprocal16.22
I(0) (reciprocal space) i0_reciprocal9223000.0000
Solution quality estimate total_estimate0.6553
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.4
Skewness Skewness skewness0.387
Kurtosis Kurtosis kurtosis-0.045
Angular range angular_range— – 0.4900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1272000.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.694; Stabil: 0.999; Sysdev: 0.485; Positv: 1.000; Valcen: 0.980; 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_idd1a1ha1
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_idd1a1ha2
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_idd1a1ha3
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_id1a1hA01
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_id1a1hA02
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_id1a1hA03
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)