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1ard

STRUCTURES OF DNA-BINDING MUTANT ZINC FINGER DOMAINS: IMPLICATIONS FOR DNA BINDING

Method: SOLUTION NMR Dmax: 41.2 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

YEAST TRANSCRIPTION FACTOR ADR1

Saccharomyces cerevisiae

UniProt P07248

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 102–130 Not recorded ZN ZINC ION × 1 SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 1ARD Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1ARE STRUCTURES OF DNA-BINDING MUTANT ZINC FINGER DOMAINS: IMPLICATIONS FOR DNA BINDING Deposited 1993-10-01 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 102–130（29 aa）
Not recorded ZN ZINC ION × 1 SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1ARF STRUCTURES OF DNA-BINDING MUTANT ZINC FINGER DOMAINS: IMPLICATIONS FOR DNA BINDING Deposited 1993-10-01 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 102–130（29 aa）
Not recorded ZN ZINC ION × 1 SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1PAA STRUCTURE OF A HISTIDINE-X4-HISTIDINE ZINC FINGER DOMAIN: INSIGHTS INTO ADR1-UAS1 PROTEIN-DNA RECOGNITION Deposited 1994-07-15 Different construct Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 130–159（30 aa）
Not recorded ZN ZINC ION × 1 SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
2ADR ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES Deposited 1998-03-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 102–161（60 aa） Fragment：DNA-BINDING DOMAIN
Mutation：C140A ZN ZINC ION × 2 SOLUTION NMR
NMR measurement conditions pH 5.5；303 K
Resolution not provided
5A7U Single-particle cryo-EM of co-translational folded adr1 domain inside the E. coli ribosome exit tunnel. Deposited 2015-07-10 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 130–158（29 aa） Fragment：RESIDUES 130-158
Not recorded ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer 20 MM HEPES PH 7.2 , 50 MM KOAC, 5 MM MG OAC2, 0.03% DDM, 50 MICROM ZNCL2, 125 MM SUCROSE.；pH 7.2；20 MM HEPES PH 7.2 , 50 MM KOAC, 5 MM MG OAC2, 0.03% DDM, 50 MICROM ZNCL2, 125 MM SUCROSE.
cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, INSTRUMENT- FEI VITROBOT MARK IV,
Resolution 4.80 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ADR1_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–29； UniProt 102–130

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 1ard

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ard
Deposition date deposition_date1993-10-01
Structure title titleSTRUCTURES OF DNA-BINDING MUTANT ZINC FINGER DOMAINS: IMPLICATIONS FOR DNA BINDING
Keywords keywordsTRANSCRIPTION REGULATION; TRANSCRIPTION REGULATION
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier9.55 Å
Radius of gyration Rg (electron density) rg_electron9.42 Å
Forward intensity I(0) i025298000.00
Molecular weight molecular_weight36425.0 kDa
Excluded volume excluded_volume43696 ų
Envelope volume envelope_volume9860 ų
Hydration-shell volume shell_volume7630 ų
Envelope diameter envelope_diameter44.3 Å
Shell Rg shell_rg16.72 Å
Envelope Rg envelope_rg12.51 Å
Shape Rg shape_rg9.41 Å
Total Rg total_rg9.91 Å
Total atoms total_atoms4950
Residues n_residues290
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 dmax41.2 Å
Rg (real space) rg_real9.64 Å
Rg uncertainty (real space) rg_real_error0.51 Å
I(0) (real space) i0_real2.5300e+07
I(0) uncertainty (real space) i0_real_error2.7800e+05
Rg (reciprocal space) rg_reciprocal9.64 Å
I(0) (reciprocal space) i0_reciprocal25300000.0000
Solution quality estimate total_estimate0.7230
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary11.5 Å
Skewness Skewness skewness0.586
Kurtosis Kurtosis kurtosis0.431
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.382; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.280; Smooth: 0.970
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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

SCOP 2.08 (1 domains)

Domain ID domain_idd1arda_
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
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8. Citations (2)

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9. Files and Curves (10)