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1cld

DNA-binding protein

Method: SOLUTION NMR Dmax: 26.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CD2-LAC9

Kluyveromyces lactis

UniProt P08657

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 85–144 Mutation：INITIATOR MET CD CADMIUM ION × 2 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 1CLD Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3E1K Crystal structure of Kluyveromyces lactis Gal80p in complex with the acidic activation domain of Gal4p Deposited 2008-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 844–865（22 aa） Fragment：UNP residues 844-865
Chain D 844–865（22 aa） Fragment：UNP residues 844-865
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；100mM MES, 20-25% (w/v) pentaerythritol propoxylate 5/4, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.00 Å R-free 0.289
3E1K Crystal structure of Kluyveromyces lactis Gal80p in complex with the acidic activation domain of Gal4p Deposited 2008-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain F 844–865（22 aa） Fragment：UNP residues 844-865
Chain H 844–865（22 aa） Fragment：UNP residues 844-865
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；100mM MES, 20-25% (w/v) pentaerythritol propoxylate 5/4, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.00 Å R-free 0.289
3E1K Crystal structure of Kluyveromyces lactis Gal80p in complex with the acidic activation domain of Gal4p Deposited 2008-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain J 844–865（22 aa） Fragment：UNP residues 844-865
Chain L 844–865（22 aa） Fragment：UNP residues 844-865
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；100mM MES, 20-25% (w/v) pentaerythritol propoxylate 5/4, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.00 Å R-free 0.289
3E1K Crystal structure of Kluyveromyces lactis Gal80p in complex with the acidic activation domain of Gal4p Deposited 2008-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain N 844–865（22 aa） Fragment：UNP residues 844-865
Chain P 844–865（22 aa） Fragment：UNP residues 844-865
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；100mM MES, 20-25% (w/v) pentaerythritol propoxylate 5/4, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.00 Å R-free 0.289

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

View Construct and Data Evidence
UniProt name LAC9_KLULA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–61； UniProt 85–144

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 1cld

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cld
Deposition date deposition_date1995-06-06
Structure title titleDNA-binding protein
Keywords keywordsZINC-BINDING DOMAIN, TRANSCRIPTION 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_guinier7.28 Å
Radius of gyration Rg (electron density) rg_electron8.33 Å
Forward intensity I(0) i0242862000.00
Molecular weight molecular_weight116450.0 kDa
Excluded volume excluded_volume138190 ų
Envelope volume envelope_volume8042 ų
Hydration-shell volume shell_volume7157 ų
Envelope diameter envelope_diameter30.4 Å
Shell Rg shell_rg15.07 Å
Envelope Rg envelope_rg10.18 Å
Shape Rg shape_rg8.51 Å
Total Rg total_rg7.91 Å
Total atoms total_atoms15109
Residues n_residues957
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 dmax26.2 Å
Rg (real space) rg_real7.27 Å
Rg uncertainty (real space) rg_real_error0.32 Å
I(0) (real space) i0_real2.4290e+08
I(0) uncertainty (real space) i0_real_error2.4390e+06
Rg (reciprocal space) rg_reciprocal7.27 Å
I(0) (reciprocal space) i0_reciprocal242900000.0000
Solution quality estimate total_estimate0.8507
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary9.3 Å
Skewness Skewness skewness0.263
Kurtosis Kurtosis kurtosis-0.143
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5329.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.745; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 0.897
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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_idd1clda_
Class classg — Small proteins
Fold Fold foldg.38 — Zn2/Cys6 DNA-binding domain
Superfamily Superfamily superfamilyg.38.1 — Zn2/Cys6 DNA-binding domain
Family Family familyg.38.1.1 — Zn2/Cys6 DNA-binding domain
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8. Citations (2)

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9. Files and Curves (10)