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2v3s

Structural insights into the recognition of substrates and activators by the OSR1 kinase

Method: X-RAY DIFFRACTION Dmax: 68.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

SERINE/THREONINE-PROTEIN KINASE OSR1

HOMO SAPIENS

UniProt O95747

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 433–527 Not recorded SERINE/THREONINE-PROTEIN KINASE WNK4 × 1 （Q96J92） X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.70 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 433–527 Not recorded SERINE/THREONINE-PROTEIN KINASE WNK4 × 1 （Q96J92） ACT ACETATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.70 Å R-free 0.239

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 2V3S Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2VWI Structure of the OSR1 kinase, a hypertension drug target Deposited 2008-06-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–303（303 aa） Fragment：KINASE DOMAIN, RESIDUES 1-303
Chain B 1–303（303 aa） Fragment：KINASE DOMAIN, RESIDUES 1-303
Chain C 1–303（303 aa） Fragment：KINASE DOMAIN, RESIDUES 1-303
Chain D 1–303（303 aa） Fragment：KINASE DOMAIN, RESIDUES 1-303
Not recorded AU GOLD ION × 11 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.15 Å R-free 0.287
3DAK Crystal Structure of Domain-Swapped OSR1 kinase domain Deposited 2008-05-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295
Chain B 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295
Chain C 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295
Chain D 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 3350, Tri-Lithium Citrate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.25 Å R-free 0.267
3DAK Crystal Structure of Domain-Swapped OSR1 kinase domain Deposited 2008-05-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295
Chain D 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 3350, Tri-Lithium Citrate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.25 Å R-free 0.267
3DAK Crystal Structure of Domain-Swapped OSR1 kinase domain Deposited 2008-05-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295
Chain C 6–295（290 aa） Fragment：Protein kinase domain, UNP residues 6-295
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 3350, Tri-Lithium Citrate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.25 Å R-free 0.267
7OKW 1.62A X-ray crystal structure of the conserved C-terminal (CCT) of human OSR1 Deposited 2021-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 423–527（105 aa）
Chain B 423–527（105 aa）
Not recorded MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 CA CALCIUM ION × 1 MG MAGNESIUM ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；278 K；Morpheus A8: 0.06 M Divalents 0.1 M Buffer System 2 7.5 37.5 % v/v Precipitant Mix 4. Divalents:Mg chloride; Ca chloride. Buffer: pH 7.5 Sodium HEPES; MOPS (acid). Precipitants: 25% v/v MPD; 25% PEG 1000; 25% w/v PEG 3350.
Resolution 1.62 Å R-free 0.216

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

View Construct and Data Evidence
UniProt name OXSR1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–96； UniProt 433–527 Author chain B； PDBConstruct 2–96； UniProt 433–527

SERINE/THREONINE-PROTEIN KINASE WNK4

OrganismNot specified

UniProt Q96J92

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 D； UniProt 1015–1020 Fragment：RESIDUES 1015-1020 SERINE/THREONINE-PROTEIN KINASE OSR1 × 1 （O95747） X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.70 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain C； UniProt 1015–1020 Fragment：RESIDUES 1015-1020 SERINE/THREONINE-PROTEIN KINASE OSR1 × 1 （O95747） ACT ACETATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.70 Å R-free 0.239

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 2V3S Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4CH9 Crystal structure of the human KLHL3 Kelch domain in complex with a WNK4 peptide Deposited 2013-11-29 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 557–567（11 aa） Fragment：RESIDUES 557-567
Not recorded SO4 SULFATE ION × 2 EDO 1,2-ETHANEDIOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.3；293 K；SITTING-DROP VAPOUR-DIFFUSTION, 25-35 % PEG 4000, 0.2 M AMMONIUM SULPHATE, 0.1 M ACETATE (PH 4.3), 293 K
Resolution 1.84 Å R-free 0.184
4CH9 Crystal structure of the human KLHL3 Kelch domain in complex with a WNK4 peptide Deposited 2013-11-29 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 557–567（11 aa） Fragment：RESIDUES 557-567
Not recorded SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.3；293 K；SITTING-DROP VAPOUR-DIFFUSTION, 25-35 % PEG 4000, 0.2 M AMMONIUM SULPHATE, 0.1 M ACETATE (PH 4.3), 293 K
Resolution 1.84 Å R-free 0.184
4CHB Crystal structure of the human KLHL2 Kelch domain in complex with a WNK4 peptide Deposited 2013-11-29 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 557–567（11 aa） Fragment：RESIDUES 557-567
Not recorded EDO 1,2-ETHANEDIOL × 3 SO4 SULFATE ION × 2 12P DODECAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；SITTING-DROP VAPOUR-DIFFUSION, 2.5 M AMMONIUM SULPHATE, 0.1 M HEPES, 2 % PEG 400 (PH 7.2), 293 K
Resolution 1.56 Å R-free 0.194
4CHB Crystal structure of the human KLHL2 Kelch domain in complex with a WNK4 peptide Deposited 2013-11-29 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 557–567（11 aa） Fragment：RESIDUES 557-567
Not recorded EDO 1,2-ETHANEDIOL × 3 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；SITTING-DROP VAPOUR-DIFFUSION, 2.5 M AMMONIUM SULPHATE, 0.1 M HEPES, 2 % PEG 400 (PH 7.2), 293 K
Resolution 1.56 Å R-free 0.194

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

View Construct and Data Evidence
UniProt name WNK4_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 1–6； UniProt 1015–1020 Author chain D； PDBConstruct 1–6； UniProt 1015–1020

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 2v3s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2v3s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2v3s
Deposition date deposition_date2007-06-21
Structure title titleStructural insights into the recognition of substrates and activators by the OSR1 kinase
Keywords keywords;ATP-BINDING, KINASE, MAGNESIUM, METAL-BINDING, NUCLEOTIDE-BINDING, PHOSPHORYLATION, POLYMORPHISM, SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier20.72 Å
Radius of gyration Rg (electron density) rg_electron19.75 Å
Forward intensity I(0) i08752400.00
Molecular weight molecular_weight21732.0 kDa
Excluded volume excluded_volume27238 ų
Envelope volume envelope_volume33804 ų
Hydration-shell volume shell_volume15220 ų
Envelope diameter envelope_diameter70.5 Å
Shell Rg shell_rg24.77 Å
Envelope Rg envelope_rg19.73 Å
Shape Rg shape_rg19.74 Å
Total Rg total_rg20.60 Å
Total atoms total_atoms1532
Residues n_residues203
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 dmax68.6 Å
Rg (real space) rg_real20.78 Å
Rg uncertainty (real space) rg_real_error0.51 Å
I(0) (real space) i0_real8.7520e+06
I(0) uncertainty (real space) i0_real_error1.1020e+05
Rg (reciprocal space) rg_reciprocal20.77 Å
I(0) (reciprocal space) i0_reciprocal8752000.0000
Solution quality estimate total_estimate0.7929
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.9 Å
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis-0.503
Angular range angular_range— – 0.3850 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3013000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.793; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.926; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2v3sA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id2v3sB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
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8. Citations (1)

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9. Files and Curves (10)