SAXSdb — 8oio

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

Kelch-like protein 12

Homo sapiens

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 268–567	Not recorded	Pleckstrin homology domain-containing family A member 4 × 1 （Q9H4M7） EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 268–567	Not recorded	Pleckstrin homology domain-containing family A member 4 × 1 （Q9H4M7） EDO 1,2-ETHANEDIOL × 3 CL CHLORIDE ION × 1 NA SODIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 268–567	Not recorded	Pleckstrin homology domain-containing family A member 4 × 1 （Q9H4M7） EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 268–567	Not recorded	Pleckstrin homology domain-containing family A member 4 × 1 （Q9H4M7）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249

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 8OIO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2VPJ Crystal structure of the Kelch domain of human KLHL12 Deposited 2008-02-29	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 268–567（300 aa） Fragment：KELCH DOMAIN, RESIDUES 268-567	Not recorded	ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；0.2M AMMONIUM ACETATE, 0.1M SODIUM ACETATE PH4.6, 30% PEG4K	Resolution 1.85 Å R-free 0.222
6TTK Crystal structure of the kelch domain of human KLHL12 in complex with DVL1 peptide Deposited 2019-12-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 268–567（300 aa）	Not recorded	NA SODIUM ION × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；30% PEG4000, 0.2 M ammonium acetate, 0.1 M acetate pH 4.6	Resolution 2.38 Å R-free 0.251
6TTK Crystal structure of the kelch domain of human KLHL12 in complex with DVL1 peptide Deposited 2019-12-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 268–567（300 aa）	Not recorded	NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；30% PEG4000, 0.2 M ammonium acetate, 0.1 M acetate pH 4.6	Resolution 2.38 Å R-free 0.251
6TTK Crystal structure of the kelch domain of human KLHL12 in complex with DVL1 peptide Deposited 2019-12-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 268–567（300 aa）	Not recorded	NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；30% PEG4000, 0.2 M ammonium acetate, 0.1 M acetate pH 4.6	Resolution 2.38 Å R-free 0.251
6TTK Crystal structure of the kelch domain of human KLHL12 in complex with DVL1 peptide Deposited 2019-12-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 268–567（300 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；30% PEG4000, 0.2 M ammonium acetate, 0.1 M acetate pH 4.6	Resolution 2.38 Å R-free 0.251
6V7O Structural Elucidation of Peptide Binding to KLHL-12, a Substrate Specific Adapter Protein in a Cul3-Ring E3 Ligase Complex Deposited 2019-12-09	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 268–567（300 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；292 K；Sodium cacodylate, Sodium citrate	Resolution 2.90 Å R-free 0.254
6V7O Structural Elucidation of Peptide Binding to KLHL-12, a Substrate Specific Adapter Protein in a Cul3-Ring E3 Ligase Complex Deposited 2019-12-09	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 268–567（300 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；292 K；Sodium cacodylate, Sodium citrate	Resolution 2.90 Å R-free 0.254
8RBH Crystal structure of the kelch domain of human KLHL12 in complex with PEF1 peptide Deposited 2023-12-04	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 268–567（300 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M BIS-TRIS pH 5.5, 200 mM NaCl, and 30% PEG4K. (1:1)	Resolution 1.88 Å R-free 0.258
8RBH Crystal structure of the kelch domain of human KLHL12 in complex with PEF1 peptide Deposited 2023-12-04	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 268–567（300 aa）	Not recorded	NA SODIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M BIS-TRIS pH 5.5, 200 mM NaCl, and 30% PEG4K. (1:1)	Resolution 1.88 Å R-free 0.258
9Y8J Crystal structure of the Kelch domain of human KLHL12 with compound 1 Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTS 2-(1H-1,3-benzimidazol-1-yl)-N-(2-fluorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 2.70 Å R-free 0.329
9Y8K Crystal structure of the Kelch domain of human KLHL12 with compound 7k Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTR 2-(2-amino-4-methyl-1H-1,3-benzimidazol-1-yl)-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.27 Å R-free 0.191
9Y8L Crystal structure of the Kelch domain of human KLHL12 with compound 8e Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTQ 2-(2-amino-5,6-dimethyl-1H-1,3-benzimidazol-1-yl)-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.27 Å R-free 0.193
9Y8M Crystal structure of the Kelch domain of human KLHL12 with compound 8i Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTE 2-(2-amino-5-fluoro-4-methyl-1H-1,3-benzimidazol-1-yl)-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.33 Å R-free 0.178
9Y8N Crystal structure of the Kelch domain of human KLHL12 with compound 8m Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTL 2-(4-methyl-1H-imidazo[4,5-c]pyridin-1-yl)-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.31 Å R-free 0.204
9Y8O Crystal structure of the Kelch domain of human KLHL12 with compound 9c Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTM 2-(2-amino-4-methyl-1H-1,3-benzimidazol-1-yl)-N-[2,6-dichloro-4-(phenoxyacetyl)phenyl]acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.29 Å R-free 0.177
9Y8Q Crystal structure of the Kelch domain of human KLHL12 with compound 9e Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTO 2-(2-amino-4-methyl-1H-1,3-benzimidazol-1-yl)-N-(2,6-dichloro-4-{[(propan-2-yl)oxy]methyl}phenyl)acetamide × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.20 Å R-free 0.152
9Y8R Crystal structure of the Kelch domain of human KLHL12 with compound 9h Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTP 2-(2-amino-4-methyl-1H-1,3-benzimidazol-1-yl)-N-[2-chloro-4-(hydroxymethyl)-3-methylphenyl]acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.33 Å R-free 0.173
9Y8S Crystal structure of the Kelch domain of human KLHL12 with compound 9k Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTN 4-[2-(2-amino-4-methyl-1H-1,3-benzimidazol-1-yl)acetamido]-N-benzyl-3-chloro-2-methylbenzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.29 Å R-free 0.170
9Y8T Crystal structure of the Kelch domain of human KLHL12 with compound 10b Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTJ 2-{2-amino-4-[(morpholin-4-yl)methyl]-1H-1,3-benzimidazol-1-yl}-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.40 Å R-free 0.208
9Y8U Crystal structure of the Kelch domain of human KLHL12 with compound 10j Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTK 2-(4-{[(3S)-3-(4-cyanopiperidin-1-yl)pyrrolidin-1-yl]methyl}-2-methyl-1H-1,3-benzimidazol-1-yl)-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.01 Å R-free 0.141
9Y8V Crystal structure of the Kelch domain of human KLHL12 with compound 10q Deposited 2025-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTF 2-{4-[(1R,2S)-2-{[(3S)-3-(1,1-dioxo-1lambda~6~-thiomorpholin-4-yl)pyrrolidin-1-yl]methyl}cyclopropyl]-2-methyl-1H-1,3-benzimidazol-1-yl}-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.27 Å R-free 0.199

16 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	KLH12_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–301； UniProt 268–567 Author chain B； PDBConstruct 2–301； UniProt 268–567 Author chain C； PDBConstruct 2–301； UniProt 268–567 Author chain D； PDBConstruct 2–301； UniProt 268–567

Pleckstrin homology domain-containing family A member 4

OrganismNot specified

UniProt Q9H4M7

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 174–184	Not recorded	Kelch-like protein 12 × 1 （Q53G59） EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 174–184	Not recorded	Kelch-like protein 12 × 1 （Q53G59） EDO 1,2-ETHANEDIOL × 3 CL CHLORIDE ION × 1 NA SODIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 174–184	Not recorded	Kelch-like protein 12 × 1 （Q53G59） EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 174–184	Not recorded	Kelch-like protein 12 × 1 （Q53G59）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249

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 8OIO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1UPQ Crystal structure of the pleckstrin homology (PH) domain of PEPP1 Deposited 2003-10-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 45–167（123 aa） Fragment：PLECKSTRIN HOMOLOGY DOMAIN, RESIDUES 45-167	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；25% PEG 5000 MME, 0.2 M AMMONIUM SULFATE, 0.1 M MES PH 6.5	Resolution 1.48 Å R-free 0.243
1UPR Crystal structure of the PEPP1 pleckstrin homology domain in complex with Inositol 1,3,4,5-tetrakisphosphate Deposited 2003-10-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 45–167（123 aa） Fragment：PLECKSTRIN HOMOLOGY DOMAIN, RESIDUES 45-167	Not recorded	4IP INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；16% PEG 20,000, 0.1 M MES (PH 6.0)	Resolution 2.27 Å R-free 0.276

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

View Construct and Data Evidence

UniProt name	PKHA4_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–11； UniProt 174–184 Author chain F； PDBConstruct 1–11； UniProt 174–184 Author chain G； PDBConstruct 1–11； UniProt 174–184 Author chain H； PDBConstruct 1–11； UniProt 174–184

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8oio
Deposition date deposition_date	2023-03-23
Structure title title	Crystal structure of the kelch domain of human KLHL12 in complex with PLEKHA4 peptide
Keywords keywords	Inhibitor, Complex, Ligase, Interaction Motif, KLHL12, PLEKHA4; LIGASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	37.18 Å
Radius of gyration Rg (electron density) rg_electron	36.74 Å
Forward intensity I(0) i0	245753000.00
Molecular weight molecular_weight	123800.0 kDa
Excluded volume excluded_volume	153310 Å³
Envelope volume envelope_volume	197220 Å³
Hydration-shell volume shell_volume	44722 Å³
Envelope diameter envelope_diameter	122.1 Å
Shell Rg shell_rg	43.08 Å
Envelope Rg envelope_rg	35.92 Å
Shape Rg shape_rg	36.75 Å
Total Rg total_rg	37.09 Å
Total atoms total_atoms	8695
Residues n_residues	1155
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	117.1 Å
Rg (real space) rg_real	37.06 Å
Rg uncertainty (real space) rg_real_error	0.91 Å
I(0) (real space) i0_real	2.4580e+08
I(0) uncertainty (real space) i0_real_error	4.2910e+06
Rg (reciprocal space) rg_reciprocal	37.14 Å
I(0) (reciprocal space) i0_reciprocal	245800000.0000
Solution quality estimate total_estimate	0.8807
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	54.5 Å
Skewness Skewness skewness	0.118
Kurtosis Kurtosis kurtosis	-0.620
Angular range angular_range	— – 0.2150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	125000000.0000
Real-space data points n_real_points	44
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.769

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Kelch-like protein 12
Molecular weight formula_weight	32905.9 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	9157

SMQGPRTRARLGANEVLLVVGGFGSQQSPIDVVEKYDPKTQEWSFLPSITRKRRYVASVSLHDRIYVIGGYDGRSRLSSVECLDYTADEDGVWYSVAPMNVRRGLAGATTLGDMIYVSGGFDGSRRHTSMERYDPNIDQWSMLGDMQTAREGAGLVVASGVIYCLGGYDGLNILNSVEKYDPHTGHWTNVTPMATKRSGAGVALLNDHIYVVGGFDGTAHLSSVEAYNIRTDSWTTVTSMTTPRCYVGATVLRGRLYAIAGYDGNSLLSSIECYDPIIDSWEVVTSMGTQRCDAGVCVLRE

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Pleckstrin homology domain-containing family A member 4
Molecular weight formula_weight	950.0 kDa
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,G,H,E

PGGPGGPPEVS

Entity 3 Entity 3 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 4 Entity 4 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	389

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8. Citations (1)

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Unit-cell length a length_a	80.469 Å
Unit-cell length b length_b	73.086 Å
Unit-cell length c length_c	103.734 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	98.81 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	monoclinic

Resolution resolution	1.954 Å
Low-resolution limit resolution_low	79.520 Å
R factor r_factor	0.2021
R_work r_work	0.1996
R_free r_free	0.2486

fit	/app/data/saxs_computation/oi/8oio/8oio.fit
pddf	/app/data/pr_computation/oi/8oio/8oio.pr.out
profile	/app/data/saxs_computation/oi/8oio/8oio.dat

Crystal structure of the kelch domain of human KLHL12 in complex with PLEKHA4 peptide

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

Kelch-like protein 12

State in the Current Structure

Other States of the Same Protein in the Database

Pleckstrin homology domain-containing family A member 4

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)