SAXSdb — 6v7o

▼

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	Dvl3-peptide × 1	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
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 268–567	Not recorded	Dvl3-peptide × 1	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

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 6V7O	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
8OIO Crystal structure of the kelch domain of human KLHL12 in complex with PLEKHA4 peptide Deposited 2023-03-23	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	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
8OIO Crystal structure of the kelch domain of human KLHL12 in complex with PLEKHA4 peptide Deposited 2023-03-23	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	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
8OIO Crystal structure of the kelch domain of human KLHL12 in complex with PLEKHA4 peptide Deposited 2023-03-23	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	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
8OIO Crystal structure of the kelch domain of human KLHL12 in complex with PLEKHA4 peptide Deposited 2023-03-23	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	No recorded non-water small molecule	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
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 23 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

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	6v7o
Deposition date deposition_date	2019-12-09
Structure title title	Structural Elucidation of Peptide Binding to KLHL-12, a Substrate Specific Adapter Protein in a Cul3-Ring E3 Ligase Complex
Keywords keywords	E3 ligase, KLHL-12, Ubiquitination, LIGASE; LIGASE
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	26.63 Å
Radius of gyration Rg (electron density) rg_electron	25.77 Å
Forward intensity I(0) i0	64106400.00
Molecular weight molecular_weight	61102.0 kDa
Excluded volume excluded_volume	75735 Å³
Envelope volume envelope_volume	89156 Å³
Hydration-shell volume shell_volume	29339 Å³
Envelope diameter envelope_diameter	86.7 Å
Shell Rg shell_rg	32.68 Å
Envelope Rg envelope_rg	25.57 Å
Shape Rg shape_rg	25.78 Å
Total Rg total_rg	26.44 Å
Total atoms total_atoms	4297
Residues n_residues	580
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

▼

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

Maximum dimension Dmax dmax	83.1 Å
Rg (real space) rg_real	26.66 Å
Rg uncertainty (real space) rg_real_error	0.45 Å
I(0) (real space) i0_real	6.4110e+07
I(0) uncertainty (real space) i0_real_error	7.8170e+05
Rg (reciprocal space) rg_reciprocal	26.65 Å
I(0) (reciprocal space) i0_reciprocal	64110000.0000
Solution quality estimate total_estimate	0.8805
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	29.1 Å
Skewness Skewness skewness	0.370
Kurtosis Kurtosis kurtosis	-0.489
Angular range angular_range	— – 0.3000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12940000.0000
Real-space data points n_real_points	61
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.743

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

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	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4297

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	Dvl3-peptide
Molecular weight formula_weight	951.1 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

PGAPPGRDLA

▼

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	6v7oA00
Class class	2 — Mainly Beta
Architecture architecture	120 — 6 Propeller
Topology topology	10 — Neuraminidase
Homologous superfamily homologous superfamily	80 — Kelch-type beta propeller

Domain ID domain_id	6v7oB00
Class class	2 — Mainly Beta
Architecture architecture	120 — 6 Propeller
Topology topology	10 — Neuraminidase
Homologous superfamily homologous superfamily	80 — Kelch-type beta propeller

▶

8. Citations (1)

▶

Unit-cell length a length_a	42.679 Å
Unit-cell length b length_b	105.124 Å
Unit-cell length c length_c	63.148 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.18 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.900 Å
Low-resolution limit resolution_low	29.368 Å
R factor r_factor	0.2119
R_work r_work	0.2071
R_free r_free	0.2542

fit	/app/data/saxs_computation/v7/6v7o/6v7o.fit
pddf	/app/data/pr_computation/v7/6v7o/6v7o.pr.out
profile	/app/data/saxs_computation/v7/6v7o/6v7o.dat

Structural Elucidation of Peptide Binding to KLHL-12, a Substrate Specific Adapter Protein in a Cul3-Ring E3 Ligase Complex

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

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)