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2gqj

Solution structure of the two zf-C2H2 like domains(493-575) of human zinc finger protein KIAA1196

Method: SOLUTION NMR Dmax: 61.1 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Zinc finger protein KIAA1196

Homo sapiens

UniProt Q96KM6

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 493–577 Fragment：zf-C2H2 like domain ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition：1.31mM 13C, 15N-labeled protein; 20mM d-Tris-HCl (pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 0.05mM ZnCl2; 1mM IDA, 10% D2O; 90% H2O | 10% D2O; 90% H2O 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 2GQJ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8TX8 Crystal Structure of RBBP4 bound to ZNF512B peptide Deposited 2023-08-22 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 × 2 PDB declaration: dimeric
Chain D 419–430（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) FMT FORMIC ACID × 3 EDO 1,2-ETHANEDIOL × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Condition Morpheus G2 0.1 M MES/imidazole, pH 6.5, 40% v/v ethylene glycol; 20 % w/v PEG 8000, 0.1 M mixture of carboxylic acids
Resolution 2.20 Å R-free 0.244
8TX8 Crystal Structure of RBBP4 bound to ZNF512B peptide Deposited 2023-08-22 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 × 2 PDB declaration: dimeric
Chain C 419–430（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) FMT FORMIC ACID × 3 EDO 1,2-ETHANEDIOL × 4 ACT ACETATE ION × 1 OXM OXAMIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Condition Morpheus G2 0.1 M MES/imidazole, pH 6.5, 40% v/v ethylene glycol; 20 % w/v PEG 8000, 0.1 M mixture of carboxylic acids
Resolution 2.20 Å R-free 0.244

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name K1196_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 8–92； UniProt 493–577

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 2gqj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2gqj
Deposition date deposition_date2006-04-21
Structure title titleSolution structure of the two zf-C2H2 like domains(493-575) of human zinc finger protein KIAA1196
Keywords keywords;zf-C2H2 like domain, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, GENE REGULATION ;; GENE 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_guinier23.29 Å
Radius of gyration Rg (electron density) rg_electron22.88 Å
Forward intensity I(0) i0796707000.00
Molecular weight molecular_weight210750.0 kDa
Excluded volume excluded_volume253030 ų
Envelope volume envelope_volume105090 ų
Hydration-shell volume shell_volume27008 ų
Envelope diameter envelope_diameter129.3 Å
Shell Rg shell_rg37.80 Å
Envelope Rg envelope_rg36.44 Å
Shape Rg shape_rg23.04 Å
Total Rg total_rg22.80 Å
Total atoms total_atoms28480
Residues n_residues1960
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 dmax61.1 Å
Rg (real space) rg_real21.08 Å
Rg uncertainty (real space) rg_real_error0.20 Å
I(0) (real space) i0_real7.5460e+08
I(0) uncertainty (real space) i0_real_error9.0110e+06
Rg (reciprocal space) rg_reciprocal23.85 Å
I(0) (reciprocal space) i0_reciprocal796600000.0000
Solution quality estimate total_estimate0.6410
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary15.1 Å
Skewness Skewness skewness0.370
Kurtosis Kurtosis kurtosis-0.748
Angular range angular_range— – 0.3400 Å−1
Current regularization parameter α current_alpha2.2510
Highest regularization parameter α highest_alpha111600.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.012; Oscil: 0.949; Stabil: 0.987; Sysdev: 0.000; Positv: 1.000; Valcen: 0.544; Smooth: 0.000
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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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8. Citations (1)

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9. Files and Curves (10)